3o43
From Proteopedia
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- | [[ | + | ==Complex of an alpha/beta-peptide based on the gp41 CHR domain bound to gp41-5== |
+ | <StructureSection load='3o43' size='340' side='right' caption='[[3o43]], [[Resolution|resolution]] 2.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3o43]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3O43 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3O43 FirstGlance]. <br> | ||
+ | </td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene><br> | ||
+ | <tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=B3E:(3S)-3-AMINOHEXANEDIOIC+ACID'>B3E</scene>, <scene name='pdbligand=B3T:3-AMINO-2,3,5-TRIDEOXY-D-THREO-PENTONIC+ACID'>B3T</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=XCP:(1S,2S)-2-AMINOCYCLOPENTANECARBOXYLIC+ACID'>XCP</scene>, <scene name='pdbligand=XPC:(3S,4R)-4-AMINOPYRROLIDINE-3-CARBOXYLIC+ACID'>XPC</scene></td></tr> | ||
+ | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3o3x|3o3x]], [[3o3y|3o3y]], [[3o3z|3o3z]], [[3o40|3o40]], [[3o42|3o42]]</td></tr> | ||
+ | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3o43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o43 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3o43 RCSB], [http://www.ebi.ac.uk/pdbsum/3o43 PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Infection of cells by HIV depends upon profound structural rearrangements within the trimeric viral protein gp41. Critical to this process is the formation of a six-helix bundle in which a set of three N-terminal heptad repeat (NHR) helices assemble to form a core displaying long grooves that provide docking sites for three C-terminal heptad repeat (CHR) helices. We report experiments designed to discriminate between two alternative hypotheses regarding the source of affinity between individual CHR helices and the complementary groove: (1) affinity is dominated by interactions of a small cluster of side chains at one end of the CHR helix; or (2) affinity depends upon interactions distributed across the long CHR helix. We have employed two complementary experimental designs, and results from both favor the latter hypothesis. | ||
- | + | Broad Distribution of Energetically Important Contacts across an Extended Protein Interface.,Johnson LM, Horne WS, Gellman SH J Am Chem Soc. 2011 Jul 6;133(26):10038-41. Epub 2011 Jun 14. PMID:21644542<ref>PMID:21644542</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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- | == | + | |
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[[Category: Synthetic construct]] | [[Category: Synthetic construct]] | ||
[[Category: Gellman, S H.]] | [[Category: Gellman, S H.]] |
Revision as of 10:27, 28 May 2014
Complex of an alpha/beta-peptide based on the gp41 CHR domain bound to gp41-5
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