1g35: Difference between revisions

Revision as of 04:20, 1 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:1g35.png

Template:STRUCTURE 1g35

CRYSTAL STRUCTURE OF HIV-1 PROTEASE IN COMPLEX WITH INHIBITOR, AHA024CRYSTAL STRUCTURE OF HIV-1 PROTEASE IN COMPLEX WITH INHIBITOR, AHA024

Template:ABSTRACT PUBMED 11170625

About this StructureAbout this Structure

1G35 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

ReferenceReference

Synthesis and comparative molecular field analysis (CoMFA) of symmetric and nonsymmetric cyclic sulfamide HIV-1 protease inhibitors., Schaal W, Karlsson A, Ahlsen G, Lindberg J, Andersson HO, Danielson UH, Classon B, Unge T, Samuelsson B, Hulten J, Hallberg A, Karlen A, J Med Chem. 2001 Jan 18;44(2):155-69. PMID:11170625

Page seeded by OCA on Tue Jul 1 04:20:28 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:1g35.gif|left|200px]]
+{{Seed}}
+[[Image:1g35.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1g35|  PDB=1g35  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF HIV-1 PROTEASE IN COMPLEX WITH INHIBITOR, AHA024'''
+===CRYSTAL STRUCTURE OF HIV-1 PROTEASE IN COMPLEX WITH INHIBITOR, AHA024===
-==Overview==
+<!--
-We have previously reported on the unexpected flipped conformation in the cyclic sulfamide class of inhibitors. An attempt to induce a symmetric binding conformation by introducing P2/P2' substituents foreseen to bind preferentially in the S2/S2' subsite was unsuccessful. On the basis of the flipped conformation we anticipated that nonsymmetric sulfamide inhibitors, with P2/P2' side chains modified individually for the S1' and S2 subsites, should be more potent than the corresponding symmetric analogues. To test this hypothesis, a set of 18 cyclic sulfamide inhibitors (11 nonsymmetric and 7 symmetric) with different P2/P2' substituents was prepared and evaluated in an enzyme assay. To rationalize the structure-activity relationship (SAR) and enable the alignment of the nonsymmetric inhibitors, i.e., which of the P2/P2' substituents of the nonsymmetric inhibitors interact with which subsite, a CoMFA study was performed. The CoMFA model, constructed from the 18 inhibitors in this study along with seven inhibitors from previous work by our group, has successfully been used to rationalize the SAR of the cyclic sulfamide inhibitors. Furthermore, from the information presented herein, the SAR of the cyclic sulfamide class of inhibitors seems to differ from the SAR of the related cyclic urea inhibitors reported by DuPont and DuPont-Merck.
+The line below this paragraph, {{ABSTRACT_PUBMED_11170625}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11170625 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11170625}}
 ==About this Structure==
@@ Line 26: / Line 30: @@
 [[Category: Unge, T.]]
 [[Category: Protein-inhibitor complex]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:04:42 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 04:20:28 2008''