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Protein structural disorder of the envelope V3 loop contributes to the switch in human immunodeficiency virus type 1 cell tropism.

Abstract:

Human immunodeficiency virus type 1 (HIV-1) envelope gp120 is partly an intrinsically disordered (unstructured/disordered) protein as it contains regions that do not fold into well-defined protein structures. These disordered regions play important roles in HIV's life cycle, particularly, V3 loop-dependent cell entry, which determines how the virus uses two coreceptors on immune cells, the chemokine receptors CCR5 (R5), CXCR4 (X4) or both (R5X4 virus). Most infecting HIV-1 variants utilise CC...

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Publication status:
Published
Peer review status:
Peer reviewed

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Institution:
University of Oxford
Division:
MSD
Department:
NDM
Sub department:
Human Genetics Wt Centre
Role:
Author

Contributors

Role:
Editor
More from this funder
Name:
Biotechnology and Biological Sciences Research Council
Grant:
Studentship
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Name:
Medical Research Council
Grant:
G1001806/1
More from this funder
Name:
Wellcome Trust
Grant:
097820/Z/11/A
Publisher:
Public Library of Science
Journal:
PLoS One More from this journal
Volume:
12
Issue:
10
Pages:
e0185790
Publication date:
2017-10-01
Acceptance date:
2017-09-19
DOI:
EISSN:
1932-6203
Pmid:
29049306
Language:
English
Keywords:
Pubs id:
pubs:739014
UUID:
uuid:ac7474f0-754b-44a1-9e58-a914be6bc762
Local pid:
pubs:739014
Source identifiers:
739014
Deposit date:
2017-11-14

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