We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2nph

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2nph.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2nph.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nph| PDB=2nph | SCENE= }}
{{STRUCTURE_2nph| PDB=2nph | SCENE= }}
-
'''Crystal structure of HIV1 protease in situ product complex'''
+
===Crystal structure of HIV1 protease in situ product complex===
-
==Overview==
+
<!--
-
HIV-1 protease is an effective target for designing drugs against AIDS, and structural information about the true transition state and the correct mechanism can provide important inputs. We present here the three-dimensional structure of a bi-product complex between HIV-1 protease and the two cleavage product peptides AETF and YVDGAA. The structure, refined against synchrotron data to 1.65 A resolution, shows the occurrence of the cleavage reaction in the crystal, with the product peptides still held in the enzyme active site. The separation between the scissile carbon and nitrogen atoms is 2.67 A, which is shorter than a normal van der Waal separation, but it is much longer than a peptide bond length. The substrate is thus in a stage just past the G'Z intermediate described in Northrop's mechanism [Northrop DB (2001) Acc Chem Res 34:790-797]. Because the products are generated in situ, the structure, by extrapolation, can give insight into the mechanism of the cleavage reaction. Both oxygens of the generated carboxyl group form hydrogen bonds with atoms at the catalytic center: one to the OD2 atom of a catalytic aspartate and the other to the scissile nitrogen atom. The latter hydrogen bond may have mediated protonation of scissile nitrogen, triggering peptide bond cleavage. The inner oxygen atoms of the catalytic aspartates in the complex are 2.30 A apart, indicating a low-barrier hydrogen bond between them at this stage of the reaction, an observation not included in Northrop's proposal. This structure forms a template for designing mechanism-based inhibitors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17116869}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17116869 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17116869}}
==About this Structure==
==About this Structure==
Line 27: Line 31:
[[Category: Prashar, V.]]
[[Category: Prashar, V.]]
[[Category: Anti-parallel beta sheet]]
[[Category: Anti-parallel beta sheet]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:44:38 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 12:27:14 2008''

Revision as of 09:27, 28 July 2008

Image:2nph.png

Template:STRUCTURE 2nph

Crystal structure of HIV1 protease in situ product complex

Template:ABSTRACT PUBMED 17116869

About this Structure

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

Reference

Crystal structure of HIV-1 protease in situ product complex and observation of a low-barrier hydrogen bond between catalytic aspartates., Das A, Prashar V, Mahale S, Serre L, Ferrer JL, Hosur MV, Proc Natl Acad Sci U S A. 2006 Dec 5;103(49):18464-9. Epub 2006 Nov 20. PMID:17116869

Page seeded by OCA on Mon Jul 28 12:27:14 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2nph"
Personal tools