2M7W
Independently verified structure of gp41-M-MAT, a membrane associated MPER trimer from HIV-1 gp41
Summary for 2M7W
| Entry DOI | 10.2210/pdb2m7w/pdb |
| Related | 2LP7 |
| NMR Information | BMRB: 19215 |
| Descriptor | Envelope glycoprotein (1 entity in total) |
| Functional Keywords | mper, gp41, viral protein |
| Biological source | Human immunodeficiency virus 1 |
| Total number of polymer chains | 3 |
| Total formula weight | 21032.43 |
| Authors | Martin, J.W.,Reardon, P.N.,Sage, H.S.,Moses, D.S.,Munir, A.S.,Haynes, B.F.,Spicer, L.D.,Donald, B.R. (deposition date: 2013-05-01, release date: 2013-05-15, Last modification date: 2024-05-15) |
| Primary citation | Reardon, P.N.,Sage, H.,Dennison, S.M.,Martin, J.W.,Donald, B.R.,Alam, S.M.,Haynes, B.F.,Spicer, L.D. Structure of an HIV-1-neutralizing antibody target, the lipid-bound gp41 envelope membrane proximal region trimer. Proc.Natl.Acad.Sci.USA, 111:1391-1396, 2014 Cited by PubMed Abstract: The membrane proximal external region (MPER) of HIV-1 glycoprotein (gp) 41 is involved in viral-host cell membrane fusion. It contains short amino acid sequences that are binding sites for the HIV-1 broadly neutralizing antibodies 2F5, 4E10, and 10E8, making these binding sites important targets for HIV-1 vaccine development. We report a high-resolution structure of a designed MPER trimer assembled on a detergent micelle. The NMR solution structure of this trimeric domain, designated gp41-M-MAT, shows that the three MPER peptides each adopt symmetric α-helical conformations exposing the amino acid side chains of the antibody binding sites. The helices are closely associated at their N termini, bend between the 2F5 and 4E10 epitopes, and gradually separate toward the C termini, where they associate with the membrane. The mAbs 2F5 and 4E10 bind gp41-M-MAT with nanomolar affinities, consistent with the substantial exposure of their respective epitopes in the trimer structure. The traditional structure determination of gp41-M-MAT using the Xplor-NIH protocol was validated by independently determining the structure using the DISCO sparse-data protocol, which exploits geometric arrangement algorithms that guarantee to compute all structures and assignments that satisfy the data. PubMed: 24474763DOI: 10.1073/pnas.1309842111 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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