Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP

The mobility and invasion strategy of Plasmodium falciparum is governed by a protein complex known as the glideosome, which contains an actin-myosin motor. It has been shown that myosin A of the parasite (PfMyoA) is the myosin of the glideosome, and the interaction of PfMyoA with myosin tail domain...

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Autores:
Hernández, Paula C.
Morales, Liliana
Castellanos, Isabel C.
Wasserman, Moisés
Chaparro-Olaya, Jacqueline
Tipo de recurso:
Article of journal
Fecha de publicación:
2017
Institución:
Universidad El Bosque
Repositorio:
Repositorio U. El Bosque
Idioma:
eng
OAI Identifier:
oai:repositorio.unbosque.edu.co:20.500.12495/3678
Acceso en línea:
http://hdl.handle.net/20.500.12495/3678
https://doi.org/10.1007/s00436-017-5417-y
https://repositorio.unbosque.edu.co
Palabra clave:
Plasmodium falciparum
PfMyoB
Protein structure prediction
Myosin
MTIP
Molecular docking
Rights
openAccess
License
Acceso abierto
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dc.title.spa.fl_str_mv Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP
dc.title.translated.spa.fl_str_mv Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP
title Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP
spellingShingle Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP
Plasmodium falciparum
PfMyoB
Protein structure prediction
Myosin
MTIP
Molecular docking
title_short Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP
title_full Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP
title_fullStr Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP
title_full_unstemmed Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP
title_sort Myosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIP
dc.creator.fl_str_mv Hernández, Paula C.
Morales, Liliana
Castellanos, Isabel C.
Wasserman, Moisés
Chaparro-Olaya, Jacqueline
dc.contributor.author.none.fl_str_mv Hernández, Paula C.
Morales, Liliana
Castellanos, Isabel C.
Wasserman, Moisés
Chaparro-Olaya, Jacqueline
dc.contributor.orcid.none.fl_str_mv Chaparro-Olaya, Jacqueline [0000-0001-9815-3459]
dc.subject.keywords.spa.fl_str_mv Plasmodium falciparum
PfMyoB
Protein structure prediction
Myosin
MTIP
Molecular docking
topic Plasmodium falciparum
PfMyoB
Protein structure prediction
Myosin
MTIP
Molecular docking
description The mobility and invasion strategy of Plasmodium falciparum is governed by a protein complex known as the glideosome, which contains an actin-myosin motor. It has been shown that myosin A of the parasite (PfMyoA) is the myosin of the glideosome, and the interaction of PfMyoA with myosin tail domain interacting protein (MTIP) determines its correct location and its ability to function in the complex. Because PfMyoA and myosin B of P. falciparum (PfMyoB) share high sequence identity, are both small proteins without a tail domain, belong to the class XIV myosins, and are expressed in late schizonts and merozoites, we suspect that these myosins may have similar or redundant functions. Therefore, this work examined the structural similarity between PfMyoA and PfMyoB and performed a molecular docking between PfMyoB and MTIP. Three-dimensional (3D) models obtained for PfMyoA and PfMyoB achieved high scores in the structural validation programs used, and their superimposition revealed high structural similarity, supporting the hypothesis of possible similar functions for these two proteins. The 3D interaction models obtained and energy values found suggested that interaction between PfMyoB and MTIP is possible. Given the apparent abundance of PfMyoA relative to PfMyoB in the parasite, we believe that the interaction between PfMyoB and MTIP would only be detectable in specific cellular environments because under normal circumstances, it would be masked by the interaction between PfMyoA and MTIP.
publishDate 2017
dc.date.issued.none.fl_str_mv 2017
dc.date.accessioned.none.fl_str_mv 2020-08-05T13:25:38Z
dc.date.available.none.fl_str_mv 2020-08-05T13:25:38Z
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dc.type.local.none.fl_str_mv Artículo de revista
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dc.type.driver.none.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.issn.none.fl_str_mv 1432-1955
dc.identifier.uri.none.fl_str_mv http://hdl.handle.net/20.500.12495/3678
dc.identifier.doi.none.fl_str_mv https://doi.org/10.1007/s00436-017-5417-y
dc.identifier.instname.spa.fl_str_mv instname:Universidad El Bosque
dc.identifier.reponame.spa.fl_str_mv reponame:Repositorio Institucional Universidad El Bosque
dc.identifier.repourl.none.fl_str_mv https://repositorio.unbosque.edu.co
identifier_str_mv 1432-1955
instname:Universidad El Bosque
reponame:Repositorio Institucional Universidad El Bosque
url http://hdl.handle.net/20.500.12495/3678
https://doi.org/10.1007/s00436-017-5417-y
https://repositorio.unbosque.edu.co
dc.language.iso.none.fl_str_mv eng
language eng
dc.relation.ispartofseries.spa.fl_str_mv Parasitology Research, 1432-1955, Vol. 116, 2017, p. 1373–1382
dc.relation.uri.none.fl_str_mv https://link.springer.com/article/10.1007/s00436-017-5417-y
dc.rights.local.spa.fl_str_mv Acceso abierto
dc.rights.accessrights.none.fl_str_mv http://purl.org/coar/access_right/c_abf2
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dc.rights.creativecommons.none.fl_str_mv 2017-03-07
rights_invalid_str_mv Acceso abierto
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2017-03-07
eu_rights_str_mv openAccess
dc.format.mimetype.none.fl_str_mv application/pdf
dc.publisher.spa.fl_str_mv Springer
dc.publisher.journal.spa.fl_str_mv Parasitology Research
institution Universidad El Bosque
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spelling Hernández, Paula C.Morales, LilianaCastellanos, Isabel C.Wasserman, MoisésChaparro-Olaya, JacquelineChaparro-Olaya, Jacqueline [0000-0001-9815-3459]2020-08-05T13:25:38Z2020-08-05T13:25:38Z20171432-1955http://hdl.handle.net/20.500.12495/3678https://doi.org/10.1007/s00436-017-5417-yinstname:Universidad El Bosquereponame:Repositorio Institucional Universidad El Bosquehttps://repositorio.unbosque.edu.coapplication/pdfengSpringerParasitology ResearchParasitology Research, 1432-1955, Vol. 116, 2017, p. 1373–1382https://link.springer.com/article/10.1007/s00436-017-5417-yMyosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIPMyosin B of plasmodium falciparum (PfMyoB): in silico prediction of its three-dimensional structure and its possible interaction with MTIPArtículo de revistahttp://purl.org/coar/resource_type/c_6501http://purl.org/coar/resource_type/c_2df8fbb1info:eu-repo/semantics/articlehttp://purl.org/coar/version/c_970fb48d4fbd8a85Plasmodium falciparumPfMyoBProtein structure predictionMyosinMTIPMolecular dockingThe mobility and invasion strategy of Plasmodium falciparum is governed by a protein complex known as the glideosome, which contains an actin-myosin motor. It has been shown that myosin A of the parasite (PfMyoA) is the myosin of the glideosome, and the interaction of PfMyoA with myosin tail domain interacting protein (MTIP) determines its correct location and its ability to function in the complex. Because PfMyoA and myosin B of P. falciparum (PfMyoB) share high sequence identity, are both small proteins without a tail domain, belong to the class XIV myosins, and are expressed in late schizonts and merozoites, we suspect that these myosins may have similar or redundant functions. Therefore, this work examined the structural similarity between PfMyoA and PfMyoB and performed a molecular docking between PfMyoB and MTIP. Three-dimensional (3D) models obtained for PfMyoA and PfMyoB achieved high scores in the structural validation programs used, and their superimposition revealed high structural similarity, supporting the hypothesis of possible similar functions for these two proteins. The 3D interaction models obtained and energy values found suggested that interaction between PfMyoB and MTIP is possible. Given the apparent abundance of PfMyoA relative to PfMyoB in the parasite, we believe that the interaction between PfMyoB and MTIP would only be detectable in specific cellular environments because under normal circumstances, it would be masked by the interaction between PfMyoA and MTIP.Acceso abiertohttp://purl.org/coar/access_right/c_abf2info:eu-repo/semantics/openAccessAcceso abierto2017-03-07ORIGINALHernández, Paula C..pdfHernández, Paula C..pdfapplication/pdf3075137https://repositorio.unbosque.edu.co/bitstreams/404be133-483b-482f-96f4-de66bcba004a/download1b1668d422afa12139c5fa938ff4cce3MD51LICENSElicense.txtlicense.txttext/plain; charset=utf-81748https://repositorio.unbosque.edu.co/bitstreams/d66290da-3e9c-4021-8bc7-ade488f01526/download8a4605be74aa9ea9d79846c1fba20a33MD52THUMBNAILHernández, Paula C..pdf.jpgHernández, Paula C..pdf.jpgimage/jpeg5775https://repositorio.unbosque.edu.co/bitstreams/d95100e7-d415-4258-ac3a-21f56a574017/download7210a811635d1799e7c05fee5d259be7MD53TEXTHernández, Paula C..pdf.txtHernández, Paula C..pdf.txtExtracted texttext/plain48721https://repositorio.unbosque.edu.co/bitstreams/ac6c9e15-a2da-4791-b107-3f1a21cb43ea/download896725e8f04207a44f091c1b517ebe8eMD5420.500.12495/3678oai:repositorio.unbosque.edu.co:20.500.12495/36782024-02-07 02:16:28.087restrictedhttps://repositorio.unbosque.edu.coRepositorio Institucional Universidad El Bosquebibliotecas@biteca.comTk9URTogUExBQ0UgWU9VUiBPV04gTElDRU5TRSBIRVJFClRoaXMgc2FtcGxlIGxpY2Vuc2UgaXMgcHJvdmlkZWQgZm9yIGluZm9ybWF0aW9uYWwgcHVycG9zZXMgb25seS4KCk5PTi1FWENMVVNJVkUgRElTVFJJQlVUSU9OIExJQ0VOU0UKCkJ5IHNpZ25pbmcgYW5kIHN1Ym1pdHRpbmcgdGhpcyBsaWNlbnNlLCB5b3UgKHRoZSBhdXRob3Iocykgb3IgY29weXJpZ2h0Cm93bmVyKSBncmFudHMgdG8gRFNwYWNlIFVuaXZlcnNpdHkgKERTVSkgdGhlIG5vbi1leGNsdXNpdmUgcmlnaHQgdG8gcmVwcm9kdWNlLAp0cmFuc2xhdGUgKGFzIGRlZmluZWQgYmVsb3cpLCBhbmQvb3IgZGlzdHJpYnV0ZSB5b3VyIHN1Ym1pc3Npb24gKGluY2x1ZGluZwp0aGUgYWJzdHJhY3QpIHdvcmxkd2lkZSBpbiBwcmludCBhbmQgZWxlY3Ryb25pYyBmb3JtYXQgYW5kIGluIGFueSBtZWRpdW0sCmluY2x1ZGluZyBidXQgbm90IGxpbWl0ZWQgdG8gYXVkaW8gb3IgdmlkZW8uCgpZb3UgYWdyZWUgdGhhdCBEU1UgbWF5LCB3aXRob3V0IGNoYW5naW5nIHRoZSBjb250ZW50LCB0cmFuc2xhdGUgdGhlCnN1Ym1pc3Npb24gdG8gYW55IG1lZGl1bSBvciBmb3JtYXQgZm9yIHRoZSBwdXJwb3NlIG9mIHByZXNlcnZhdGlvbi4KCllvdSBhbHNvIGFncmVlIHRoYXQgRFNVIG1heSBrZWVwIG1vcmUgdGhhbiBvbmUgY29weSBvZiB0aGlzIHN1Ym1pc3Npb24gZm9yCnB1cnBvc2VzIG9mIHNlY3VyaXR5LCBiYWNrLXVwIGFuZCBwcmVzZXJ2YXRpb24uCgpZb3UgcmVwcmVzZW50IHRoYXQgdGhlIHN1Ym1pc3Npb24gaXMgeW91ciBvcmlnaW5hbCB3b3JrLCBhbmQgdGhhdCB5b3UgaGF2ZQp0aGUgcmlnaHQgdG8gZ3JhbnQgdGhlIHJpZ2h0cyBjb250YWluZWQgaW4gdGhpcyBsaWNlbnNlLiBZb3UgYWxzbyByZXByZXNlbnQKdGhhdCB5b3VyIHN1Ym1pc3Npb24gZG9lcyBub3QsIHRvIHRoZSBiZXN0IG9mIHlvdXIga25vd2xlZGdlLCBpbmZyaW5nZSB1cG9uCmFueW9uZSdzIGNvcHlyaWdodC4KCklmIHRoZSBzdWJtaXNzaW9uIGNvbnRhaW5zIG1hdGVyaWFsIGZvciB3aGljaCB5b3UgZG8gbm90IGhvbGQgY29weXJpZ2h0LAp5b3UgcmVwcmVzZW50IHRoYXQgeW91IGhhdmUgb2J0YWluZWQgdGhlIHVucmVzdHJpY3RlZCBwZXJtaXNzaW9uIG9mIHRoZQpjb3B5cmlnaHQgb3duZXIgdG8gZ3JhbnQgRFNVIHRoZSByaWdodHMgcmVxdWlyZWQgYnkgdGhpcyBsaWNlbnNlLCBhbmQgdGhhdApzdWNoIHRoaXJkLXBhcnR5IG93bmVkIG1hdGVyaWFsIGlzIGNsZWFybHkgaWRlbnRpZmllZCBhbmQgYWNrbm93bGVkZ2VkCndpdGhpbiB0aGUgdGV4dCBvciBjb250ZW50IG9mIHRoZSBzdWJtaXNzaW9uLgoKSUYgVEhFIFNVQk1JU1NJT04gSVMgQkFTRUQgVVBPTiBXT1JLIFRIQVQgSEFTIEJFRU4gU1BPTlNPUkVEIE9SIFNVUFBPUlRFRApCWSBBTiBBR0VOQ1kgT1IgT1JHQU5JWkFUSU9OIE9USEVSIFRIQU4gRFNVLCBZT1UgUkVQUkVTRU5UIFRIQVQgWU9VIEhBVkUKRlVMRklMTEVEIEFOWSBSSUdIVCBPRiBSRVZJRVcgT1IgT1RIRVIgT0JMSUdBVElPTlMgUkVRVUlSRUQgQlkgU1VDSApDT05UUkFDVCBPUiBBR1JFRU1FTlQuCgpEU1Ugd2lsbCBjbGVhcmx5IGlkZW50aWZ5IHlvdXIgbmFtZShzKSBhcyB0aGUgYXV0aG9yKHMpIG9yIG93bmVyKHMpIG9mIHRoZQpzdWJtaXNzaW9uLCBhbmQgd2lsbCBub3QgbWFrZSBhbnkgYWx0ZXJhdGlvbiwgb3RoZXIgdGhhbiBhcyBhbGxvd2VkIGJ5IHRoaXMKbGljZW5zZSwgdG8geW91ciBzdWJtaXNzaW9uLgo=