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PDBsum entry 5a8h
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Viral protein/immune system
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PDB id
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5a8h
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Contents |
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306 a.a.
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181 a.a.
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214 a.a.
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229 a.a.
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214 a.a.
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224 a.a.
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PDB id:
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| Name: |
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Viral protein/immune system
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Title:
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Cryo-et subtomogram averaging of bg505 sosip.664 in complex with scd4, 17b, and 8anc195
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Structure:
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HIV-1 gp120. Chain: a, g, m. Engineered: yes. T-cell surface glycoprotein cd4. Chain: b, h, n. Fragment: soluble cd4 d1-d2 domains, residues26-208. Synonym: t-cell surface antigen t4/leu-3, cd4. Engineered: yes. Fab of broadly neutralizing antibody 17b.
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Source:
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Human immunodeficiency virus 1. HIV-1. Organism_taxid: 11676. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek-6e. Homo sapiens. Human. Organism_taxid: 9606.
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Authors:
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L.Scharf,H.Wang,H.Gao,S.Chen,A.Mcdowall,P.Bjorkman
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Key ref:
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L.Scharf
et al.
(2015).
Broadly Neutralizing Antibody 8ANC195 Recognizes Closed and Open States of HIV-1 Env.
Cell,
162,
1379-1390.
PubMed id:
DOI:
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Date:
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15-Jul-15
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Release date:
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05-Aug-15
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PROCHECK
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Headers
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References
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P35961
(ENV_HV1Y2) -
Envelope glycoprotein gp160 from Human immunodeficiency virus type 1 group M subtype B (isolate YU-2)
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Seq:
Struc:
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843 a.a.
306 a.a.*
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P01730
(CD4_HUMAN) -
T-cell surface glycoprotein CD4 from Homo sapiens
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Seq:
Struc:
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458 a.a.
181 a.a.
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No UniProt id for this chain
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No UniProt id for this chain
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DOI no:
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Cell
162:1379-1390
(2015)
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PubMed id:
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Broadly Neutralizing Antibody 8ANC195 Recognizes Closed and Open States of HIV-1 Env.
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L.Scharf,
H.Wang,
H.Gao,
S.Chen,
A.W.McDowall,
P.J.Bjorkman.
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ABSTRACT
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The HIV-1 envelope (Env) spike contains limited epitopes for broadly
neutralizing antibodies (bNAbs); thus, most neutralizing antibodies are strain
specific. The 8ANC195 epitope, defined by crystal and electron microscopy (EM)
structures of bNAb 8ANC195 complexed with monomeric gp120 and trimeric Env,
respectively, spans the gp120 and gp41 Env subunits. To investigate 8ANC195's
gp41 epitope at higher resolution, we solved a 3.58 Å crystal structure of
8ANC195 complexed with fully glycosylated Env trimer, revealing 8ANC195
insertion into a glycan shield gap to contact gp120 and gp41 glycans and protein
residues. To determine whether 8ANC195 recognizes the CD4-bound open Env
conformation that leads to co-receptor binding and fusion, one of several known
conformations of virion-associated Env, we solved EM structures of an
Env/CD4/CD4-induced antibody/8ANC195 complex. 8ANC195 binding partially closed
the CD4-bound trimer, confirming structural plasticity of Env by revealing a
previously unseen conformation. 8ANC195's ability to bind different Env
conformations suggests advantages for potential therapeutic applications.
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