This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2hb4

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2hb4.gif|left|200px]]
+
{{Seed}}
 +
[[Image:2hb4.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2hb4| PDB=2hb4 | SCENE= }}
{{STRUCTURE_2hb4| PDB=2hb4 | SCENE= }}
-
'''Structure of HIV Protease NL4-3 in an Unliganded State'''
+
===Structure of HIV Protease NL4-3 in an Unliganded State===
-
==Overview==
+
<!--
-
The crystal structures of wild-type HIV protease (HIV PR) in the absence of substrate or inhibitor in two related crystal forms at 1.4 and 2.15 A resolution are reported. In one crystal form HIV PR adopts an 'open' conformation with a 7.7 A separation between the tips of the flaps in the homodimer. In the other crystal form the tips of the flaps are 'curled' towards the 80s loop, forming contacts across the local twofold axis. The 2.3 A resolution crystal structure of a sixfold mutant of HIV PR in the absence of substrate or inhibitor is also reported. The mutant HIV PR, which evolved in response to treatment with the potent inhibitor TL-3, contains six point mutations relative to the wild-type enzyme (L24I, M46I, F53L, L63P, V77I, V82A). In this structure the flaps also adopt a 'curled' conformation, but are separated and not in contact. Comparison of the apo structures to those with TL-3 bound demonstrates the extent of conformational change induced by inhibitor binding, which includes reorganization of the packing between twofold-related flaps. Further comparison with six other apo HIV PR structures reveals that the 'open' and 'curled' conformations define two distinct families in HIV PR. These conformational states include hinge motion of residues at either end of the flaps, opening and closing the entire beta-loop, and translational motion of the flap normal to the dimer twofold axis and relative to the 80s loop. The alternate conformations also entail changes in the beta-turn at the tip of the flap. These observations provide insight into the plasticity of the flap domains, the nature of their motions and their critical role in binding substrates and inhibitors.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17642513}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17642513 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17642513}}
==About this Structure==
==About this Structure==
Line 31: Line 35:
[[Category: Protease]]
[[Category: Protease]]
[[Category: Retrovirus]]
[[Category: Retrovirus]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:04:44 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:34:57 2008''

Revision as of 10:34, 29 July 2008

Image:2hb4.png

Template:STRUCTURE 2hb4

Structure of HIV Protease NL4-3 in an Unliganded State

Template:ABSTRACT PUBMED 17642513

About this Structure

2HB4 is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Conformational flexibility in the flap domains of ligand-free HIV protease., Heaslet H, Rosenfeld R, Giffin M, Lin YC, Tam K, Torbett BE, Elder JH, McRee DE, Stout CD, Acta Crystallogr D Biol Crystallogr. 2007 Aug;63(Pt 8):866-75. Epub 2007, Jul 17. PMID:17642513

Page seeded by OCA on Tue Jul 29 13:34:57 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2hb4"
Personal tools