From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:2pc0.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:2pc0.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_2pc0| PDB=2pc0 | SCENE= }} | | {{STRUCTURE_2pc0| PDB=2pc0 | SCENE= }} |
| | | | |
| - | '''Apo Wild-type HIV Protease in the open conformation'''
| + | ===Apo Wild-type HIV Protease in the open conformation=== |
| | | | |
| | | | |
| - | ==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 30: |
Line 34: |
| | [[Category: Stout, C D.]] | | [[Category: Stout, C D.]] |
| | [[Category: Hiv protease]] | | [[Category: Hiv protease]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:48:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:52:50 2008'' |
Revision as of 16:53, 27 July 2008
Template:STRUCTURE 2pc0
Apo Wild-type HIV Protease in the open conformation
Template:ABSTRACT PUBMED 17642513
About this Structure
2PC0 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 Sun Jul 27 19:52:50 2008
