3O43
Complex of an alpha/beta-peptide based on the gp41 CHR domain bound to gp41-5
Summary for 3O43
| Entry DOI | 10.2210/pdb3o43/pdb |
| Related | 3O3X 3O3Y 3O3Z 3O40 3O42 |
| Descriptor | gp41-5, alpha/beta-peptide derived from gp41 CHR domain sequence, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | hiv fusion inhibitor, mixed alpha-peptide/beta-peptide backbone, viral protein |
| Biological source | Artificial gene More |
| Total number of polymer chains | 2 |
| Total formula weight | 27141.28 |
| Authors | Horne, W.S.,Johnson, L.M.,Gellman, S.H. (deposition date: 2010-07-26, release date: 2011-07-27, Last modification date: 2023-11-15) |
| Primary citation | Johnson, L.M.,Horne, W.S.,Gellman, S.H. Broad Distribution of Energetically Important Contacts across an Extended Protein Interface. J.Am.Chem.Soc., 133:10038-10041, 2011 Cited by PubMed Abstract: 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. PubMed: 21644542DOI: 10.1021/ja203358t PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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