2hvp: Difference between revisions

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|ACTIVITY=  
|ACTIVITY=  
|GENE=  
|GENE=  
|DOMAIN=
|RELATEDENTRY=
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hvp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hvp OCA], [http://www.ebi.ac.uk/pdbsum/2hvp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2hvp RCSB]</span>
}}
}}


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[[Category: hydrolase(acid proteinase)]]
[[Category: hydrolase(acid proteinase)]]


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Revision as of 00:36, 31 March 2008

File:2hvp.gif


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2hvp, resolution 3.0Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



THREE-DIMENSIONAL STRUCTURE OF ASPARTYL PROTEASE FROM HUMAN IMMUNODEFICIENCY VIRUS HIV-1


Overview

The crystal structure of the protease of the human immunodeficiency virus type (HIV-1), which releases structural proteins and enzymes from viral polyprotein products, has been determined to 3 A resolution. Large regions of the protease dimer, including the active site, have structural homology to the family of microbial aspartyl proteases. The structure suggests a mechanism for the autoproteolytic release of protease and a role in the control of virus maturation.

About this Structure

2HVP is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Three-dimensional structure of aspartyl protease from human immunodeficiency virus HIV-1., Navia MA, Fitzgerald PM, McKeever BM, Leu CT, Heimbach JC, Herber WK, Sigal IS, Darke PL, Springer JP, Nature. 1989 Feb 16;337(6208):615-20. PMID:2645523

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