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4NCO

Crystal Structure of the BG505 SOSIP gp140 HIV-1 Env trimer in Complex with the Broadly Neutralizing Fab PGT122

Summary for 4NCO
Entry DOI10.2210/pdb4nco/pdb
Related3J5M 4JY4 4JY5 4JY6
Related PRD IDPRD_900111
DescriptorBG505 SOSIP gp120, BG505 SOSIP gp41, PGT122 light chain, ... (8 entities in total)
Functional Keywordstype-1 membrane fusion glycoprotein trimer, hiv-1 envelope, gp120, gp41, membrane fusion, viral entry, cd4, ccr5/cxcr4, broadly neutralizing antibodies, viral surface, viral protein-immune system complex, viral protein/immune system
Biological sourceHuman immunodeficiency virus 1
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Total number of polymer chains12
Total formula weight350934.77
Authors
Julien, J.-P.,Stanfield, R.L.,Lyumkis, D.,Ward, A.B.,Wilson, I.A. (deposition date: 2013-10-24, release date: 2013-11-13, Last modification date: 2024-11-20)
Primary citationJulien, J.P.,Cupo, A.,Sok, D.,Stanfield, R.L.,Lyumkis, D.,Deller, M.C.,Klasse, P.J.,Burton, D.R.,Sanders, R.W.,Moore, J.P.,Ward, A.B.,Wilson, I.A.
Crystal structure of a soluble cleaved HIV-1 envelope trimer.
Science, 342:1477-1483, 2013
Cited by
PubMed Abstract: HIV-1 entry into CD4(+) target cells is mediated by cleaved envelope glycoprotein (Env) trimers that have been challenging to characterize structurally. Here, we describe the crystal structure at 4.7 angstroms of a soluble, cleaved Env trimer that is stabilized and antigenically near-native (termed the BG505 SOSIP.664 gp140 trimer) in complex with a potent broadly neutralizing antibody, PGT122. The structure shows a prefusion state of gp41, the interaction between the component gp120 and gp41 subunits, and how a close association between the gp120 V1/V2/V3 loops stabilizes the trimer apex around the threefold axis. The complete epitope of PGT122 on the trimer involves gp120 V1, V3, and several surrounding glycans. This trimer structure advances our understanding of how Env functions and is presented to the immune system, and provides a blueprint for structure-based vaccine design.
PubMed: 24179159
DOI: 10.1126/science.1245625
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4.7 Å)
Structure validation

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