3o43

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'''Unreleased structure'''
 
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The entry 3o43 is ON HOLD until Paper Publication
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==Complex of an alpha/beta-peptide based on the gp41 CHR domain bound to gp41-5==
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<StructureSection load='3o43' size='340' side='right'caption='[[3o43]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[3o43]] is a 2 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=3O43 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=GOL:GLYCEROL'>GOL</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>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3o43 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3o43 OCA], [https://pdbe.org/3o43 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3o43 RCSB], [https://www.ebi.ac.uk/pdbsum/3o43 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3o43 ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Horne, W.S., Johnson, L.M., Gellman, S.H.
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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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Description: Complex of an alpha/beta-peptide based on the gp41 CHR domain bound to gp41-5
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug 18 11:24:43 2010''
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<div class="pdbe-citations 3o43" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Gellman SH]]
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[[Category: Horne WS]]
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[[Category: Johnson LM]]

Current revision

Complex of an alpha/beta-peptide based on the gp41 CHR domain bound to gp41-5

PDB ID 3o43

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