2Q3I
Crystal structure of the D10-P3/IQN17 complex: a D-peptide inhibitor of HIV-1 entry bound to the GP41 coiled-coil pocket
Summary for 2Q3I
| Entry DOI | 10.2210/pdb2q3i/pdb |
| Related | 1CZQ |
| Descriptor | Fusion protein between the Coiled-Coil pocket of HIV GP41 and gcn4-PIQI, D-peptide, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | envelope glycoprotein, viral protein-inhibitor complex, viral protein/inhibitor |
| Total number of polymer chains | 2 |
| Total formula weight | 7271.01 |
| Authors | Malashkevich, V.N.,Eckert, D.M.,Hong, L.H.,Carr, P.A.,Kim, P.S. (deposition date: 2007-05-30, release date: 2007-06-12, Last modification date: 2024-11-13) |
| Primary citation | Eckert, D.M.,Malashkevich, V.N.,Hong, L.H.,Carr, P.A.,Kim, P.S. Inhibiting HIV Entry: Discovery of D-Peptide Inhibitors that Target the Gp41 Coiled-Coil Pocket Cell(Cambridge,Mass.), 99:103-105, 1999 Cited by PubMed Abstract: The HIV-1 gp41 protein promotes viral entry by mediating the fusion of viral and cellular membranes. A prominent pocket on the surface of a central trimeric coiled coil within gp41 was previously identified as a potential target for drugs that inhibit HIV-1 entry. We designed a peptide, IQN17, which properly presents this pocket. Utilizing IQN17 and mirror-image phage display, we identified cyclic, D-peptide inhibitors of HIV-1 infection that share a sequence motif. A 1.5 A cocrystal structure of IQN17 in complex with a D-peptide, and NMR studies, show that conserved residues of these inhibitors make intimate contact with the gp41 pocket. Our studies validate the pocket per se as a target for drug development. IQN17 and these D-peptide inhibitors are likely to be useful for development and identification of a new class of orally bioavailable anti-HIV drugs. PubMed: 10520998DOI: 10.1016/S0092-8674(00)80066-5 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.5 Å) |
Structure validation
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