2qnp: Difference between revisions

Revision as of 17:07, 28 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:2qnp.png

Template:STRUCTURE 2qnp

HIV-1 Protease in complex with a iodo decorated pyrrolidine-based inhibitorHIV-1 Protease in complex with a iodo decorated pyrrolidine-based inhibitor

Template:ABSTRACT PUBMED 18348517

About this StructureAbout this Structure

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

ReferenceReference

Structure-Guided Design of C2-Symmetric HIV-1 Protease Inhibitors Based on a Pyrrolidine Scaffold., Blum A, Bottcher J, Heine A, Klebe G, Diederich WE, J Med Chem. 2008 Apr 10;51(7):2078-87. Epub 2008 Mar 19. PMID:18348517

Page seeded by OCA on Mon Jul 28 17:07:11 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''HIV-1 Protease in complex with a iodo decorated pyrrolidine-based inhibitor'''
+===HIV-1 Protease in complex with a iodo decorated pyrrolidine-based inhibitor===
-==Overview==
+<!--
-Infections with the human immunodeficiency virus, which inevitably lead to the development of AIDS, are still among the most serious global health problems causing more than 2.5 million deaths per year. In the pathophysiological processes of this pandemic, HIV protease has proven to be an invaluable drug target because of its essential role in the virus' replication process. By use of pyrrolidine as core structure, symmetric 3,4-bis- N-alkylsulfonamides were designed and synthesized enantioselectively from d-(-)-tartaric acid as a new class of HIV protease inhibitors. Structure-guided design using the cocrystal structure of an initial lead as starting point resulted in a second series of inhibitors with improved affinity. The binding modes of four representatives were determined by X-ray crystallography to elucidate the underlying factors accounting for the SAR. With this information for further rational design, the combination of suitable side chains resulted in a final inhibitor showing a significantly improved affinity of K i = 74 nM.
+The line below this paragraph, {{ABSTRACT_PUBMED_18348517}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 18348517 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_18348517}}
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