3o40

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

spinqualitylabelsall models 3o40, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3o40 is a 2 chain structure with sequence from Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.1Å Ligands: 2PE, ACE, B3E, B3T, CL, GOL, NH2, XCP, XPC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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