2r8n: Difference between revisions
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==Structural Analysis of the Unbound Form of HIV-1 Subtype C Protease== | ==Structural Analysis of the Unbound Form of HIV-1 Subtype C Protease== | ||
<StructureSection load='2r8n' size='340' side='right' caption='[[2r8n]], [[Resolution|resolution]] 1.20Å' scene=''> | <StructureSection load='2r8n' size='340' side='right' caption='[[2r8n]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
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<table><tr><td colspan='2'>[[2r8n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R8N FirstGlance]. <br> | <table><tr><td colspan='2'>[[2r8n]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2R8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2R8N FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id= Human immunodeficiency virus 1])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pol ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r8n OCA], [http://pdbe.org/2r8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r8n RCSB], [http://www.ebi.ac.uk/pdbsum/2r8n PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2r8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2r8n OCA], [http://pdbe.org/2r8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2r8n RCSB], [http://www.ebi.ac.uk/pdbsum/2r8n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2r8n ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
Revision as of 10:45, 25 October 2017
Structural Analysis of the Unbound Form of HIV-1 Subtype C ProteaseStructural Analysis of the Unbound Form of HIV-1 Subtype C Protease
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 PubMedThe X-ray crystal structure of the unbound state of human immunodeficiency virus 1 (HIV-1) subtype C protease (C PR) has been determined to 1.20 angstroms resolution in the tetragonal space group P4(1)2(1)2, with one monomer per asymmetric unit and unit-cell parameters a = 46.7, c = 100.8 angstroms, allowing full anisotropic least-squares refinement. The refined model has a conventional R factor of 14.1% for all reflections and estimated standard deviations in bond lengths and angles for all main-chain non-H atoms of 0.014 angstroms and 0.030 degrees , respectively. The structure is compared with three unbound subtype B proteases (B PRs) to identify structural changes arising from the naturally occurring polymorphisms and delineate their implications in antiretroviral drug resistance/susceptibility. The unbound C PR exhibits a larger distance between the tips of the flaps, a downward displacement of the 36-41 loop and an increased thermal stability of the 10s loop when compared with the B PR structures. The C PR structure presents the highest resolution of the unbound state of a non-subtype-B PR and adds to the understanding of flap dynamics and drug resistance. High-resolution structure of unbound human immunodeficiency virus 1 subtype C protease: implications of flap dynamics and drug resistance.,Coman RM, Robbins AH, Goodenow MM, Dunn BM, McKenna R Acta Crystallogr D Biol Crystallogr. 2008 Jul;D64(Pt 7):754-63. Epub 2008, Jun 18. PMID:18566511[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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