1qbz: Difference between revisions
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<StructureSection load='1qbz' size='340' side='right'caption='[[1qbz]], [[Resolution|resolution]] 1.47Å' scene=''> | <StructureSection load='1qbz' size='340' side='right'caption='[[1qbz]], [[Resolution|resolution]] 1.47Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1qbz]] is a 3 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1qbz]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Civ Civ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QBZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QBZ FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=HG:MERCURY+(II)+ION'>HG</scene>, <scene name='pdbligand=MRD:(4R)-2-METHYLPENTANE-2,4-DIOL'>MRD</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qbz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qbz OCA], [https://pdbe.org/1qbz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qbz RCSB], [https://www.ebi.ac.uk/pdbsum/1qbz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qbz ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 12:40, 8 September 2021
THE CRYSTAL STRUCTURE OF THE SIV GP41 ECTODOMAIN AT 1.47 ATHE CRYSTAL STRUCTURE OF THE SIV GP41 ECTODOMAIN AT 1.47 A
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedCell membrane fusion by human (HIV) and simian (SIV) immunodeficiency viruses is mediated by the envelope glycoproteins gp120 and gp41. Although the precise mechanism of the fusion process is unknown, the ectodomain of gp41 is thought to undergo dramatic rearrangement from its prefusogenic state. To elucidate this process further, the crystal structure of the SIV gp41 ectodomain (residues 27-149) was determined at 1.47 A resolution and is reported herein. It is the most accurate and complete structure of a retroviral gp41 ectodomain determined to date. The rod-like trimeric structure of SIV gp41 comprises three parallel N-terminal alpha-helices assembled as a coiled coil in the center with three antiparallel C-terminal alpha-helices packed on the outside connected by highly flexible loops. Portions of the loops in all three monomers are crystallographically disordered and could not be accurately modeled. The core of the structure is similar (but not identical) to those of smaller HIV/SIV gp41 segments previously determined by X-ray crystallography with root mean square deviations in main chain atoms of less than 1.0 A. The crystal structure differs more substantially from the reported NMR solution structure of the identical SIV construct. The mechanisms of viral fusion and the inhibition by peptides are discussed in the context of the three-dimensional structure. The crystal structure of the SIV gp41 ectodomain at 1.47 A resolution.,Yang ZN, Mueser TC, Kaufman J, Stahl SJ, Wingfield PT, Hyde CC J Struct Biol. 1999 Jun 15;126(2):131-44. PMID:10388624[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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