1nh0

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{{STRUCTURE_1nh0| PDB=1nh0 | SCENE= }}
{{STRUCTURE_1nh0| PDB=1nh0 | SCENE= }}
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'''1.03 A structure of HIV-1 protease: inhibitor binding inside and outside the active site'''
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===1.03 A structure of HIV-1 protease: inhibitor binding inside and outside the active site===
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==Overview==
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The X-ray structure of a complex of HIV-1 protease (PR) with a phenylnorstatine inhibitor Z-Pns-Phe-Glu-Glu-NH(2) has been determined at 1.03 A, the highest resolution so far reported for any HIV PR complex. The inhibitor shows subnanomolar K(i) values for both the wild-type PR and the variant representing one of the most common mutations linked to resistance development. The structure comprising the phenylnorstatine moiety of (2R,3S)-chirality displays a unique pattern of hydrogen bonding to the two catalytic aspartate residues. This high resolution makes it possible to assess the donor and acceptor relations of this hydrogen bonding and to indicate a proton shared by the two catalytic residues. A structural mechanism for the unimpaired inhibition of the protease Val82Ala mutant is also suggested, based on energy calculations and analyses.
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(as it appears on PubMed at http://www.pubmed.gov), where 15056001 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15056001}}
==About this Structure==
==About this Structure==
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[[Category: Human immunodeficiency virus]]
[[Category: Human immunodeficiency virus]]
[[Category: Inhibitor design]]
[[Category: Inhibitor design]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:31:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:00:52 2008''

Revision as of 03:00, 28 July 2008

Template:STRUCTURE 1nh0

1.03 A structure of HIV-1 protease: inhibitor binding inside and outside the active site

Template:ABSTRACT PUBMED 15056001

About this Structure

1NH0 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

A phenylnorstatine inhibitor binding to HIV-1 protease: geometry, protonation, and subsite-pocket interactions analyzed at atomic resolution., Brynda J, Rezacova P, Fabry M, Horejsi M, Stouracova R, Sedlacek J, Soucek M, Hradilek M, Lepsik M, Konvalinka J, J Med Chem. 2004 Apr 8;47(8):2030-6. PMID:15056001

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