1kjf: Difference between revisions

Revision as of 10:25, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1kjf.png

Template:STRUCTURE 1kjf

SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXESSUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES

Template:ABSTRACT PUBMED 12005435

About this StructureAbout this Structure

1KJF is a Protein complex structure of sequences from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

ReferenceReference

Substrate shape determines specificity of recognition for HIV-1 protease: analysis of crystal structures of six substrate complexes., Prabu-Jeyabalan M, Nalivaika E, Schiffer CA, Structure. 2002 Mar;10(3):369-81. PMID:12005435

Page seeded by OCA on Wed Jul 2 10:25:42 2008

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OCA

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-'''SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES'''
+===SUBSTRATE SHAPE DETERMINES SPECIFICITY OF RECOGNITION RECOGNITION FOR HIV-1 PROTEASE: ANALYSIS OF CRYSTAL STRUCTURES OF SIX SUBSTRATE COMPLEXES===
-==Overview==
+<!--
-The homodimeric HIV-1 protease is the target of some of the most effective antiviral AIDS therapy, as it facilitates viral maturation by cleaving ten asymmetric and nonhomologous sequences in the Gag and Pol polyproteins. Since the specificity of this enzyme is not easily determined from the sequences of these cleavage sites alone, we solved the crystal structures of complexes of an inactive variant (D25N) of HIV-1 protease with six peptides that correspond to the natural substrate cleavage sites. When the protease binds to its substrate and buries nearly 1000 A2 of surface area, the symmetry of the protease is broken, yet most internal hydrogen bonds and waters are conserved. However, no substrate side chain hydrogen bond is conserved. Specificity of HIV-1 protease appears to be determined by an asymmetric shape rather than a particular amino acid sequence.
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+{{ABSTRACT_PUBMED_12005435}}
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 [[Category: P1-p6]]
 [[Category: Substrate recognition]]
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