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Kang, Sebyung
Protein Nanobio Lab
Research Interests
  • Protein engineering, Drug/diagnostics delivery nanoplatform, Protein-based vaccine delivery systems, Biosensor & imaging

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A Retroviral Chimeric Capsid Protein Reveals the Role of the N-Terminal beta-Hairpin in Mature Core Assembly

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dc.contributor.author Cortines, Juliana R. ko
dc.contributor.author Monroe, Eric B. ko
dc.contributor.author Kang, Sebyung ko
dc.contributor.author Prevelige, Peter E., Jr. ko
dc.date.available 2014-04-10T02:18:33Z -
dc.date.created 2013-06-07 ko
dc.date.issued 2011-07 ko
dc.identifier.citation JOURNAL OF MOLECULAR BIOLOGY, v.410, no.4, pp.641 - 652 ko
dc.identifier.issn 0022-2836 ko
dc.identifier.uri https://scholarworks.unist.ac.kr/handle/201301/3721 -
dc.description.abstract The human immunodeficiency virus (HIV) is an enveloped virus constituted by two monomeric RNA molecules that encode for 15 proteins. Among these are the structural proteins that are translated as the gag polyprotein. In order to become infectious, HIV must undergo a maturation process mediated by the proteolytic cleavage of gag to give rise to the isolated structural protein matrix, capsid (CA), nucleocapsid as well as p6 and spacer peptides 1 and 2. Upon maturation, the 13 N-terminal residues from CA fold into a beta-hairpin, which is stabilized mainly by a salt bridge between Prol and Asp51. Previous reports have shown that non-formation of the salt bridge, which potentially disrupts proper beta-hairpin arrangement, generates noninfectious virus or aberrant cores. To date, however, there is no consensus on the role of the beta-hairpin. In order to shed light in this subject, we have generated mutations in the hairpin region to examine what features would be crucial for the beta-hairpin's role in retroviral mature core formation. These features include the importance of the proline at the N-terminus, the amino acid sequence, and the physical structure of the beta-hairpin itself. The presented experiments provide biochemical evidence that beta-hairpin formation plays an important role in regard to CA protein conformation required to support proper mature core arrangement. Hydrogen/deuterium exchange and in vitro assembly reactions illustrated the importance of the beta-hairpin structure, its dynamics, and its influence on the orientation of helix 1 for the assembly of the mature CA lattice. ko
dc.description.statementofresponsibility close -
dc.language 영어 ko
dc.publisher ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD ko
dc.title A Retroviral Chimeric Capsid Protein Reveals the Role of the N-Terminal beta-Hairpin in Mature Core Assembly ko
dc.type ARTICLE ko
dc.identifier.scopusid 2-s2.0-80051768952 ko
dc.identifier.wosid 000293674000012 ko
dc.type.rims ART ko
dc.description.wostc 11 *
dc.description.scopustc 8 *
dc.date.tcdate 2015-02-28 *
dc.date.scptcdate 2014-07-12 *
dc.identifier.doi 10.1016/j.jmb.2011.03.052 ko
dc.identifier.url http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=80051768952 ko
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