4NUG

Crystal structure of HIV-1 broadly neutralizing antibody PGT151

Summary for 4NUG

• Entry DOI: 10.2210/pdb4nug/pdb
• Descriptor: PGT151 light chain, PGT151 heavy chain, HEXAETHYLENE GLYCOL, ... (4 entities in total)
• Functional Keywords: immunoglobulin, fab fragment, immune system, hiv envelope
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 50709.91

Authors

Blattner, C.,Wilson, I.A. (deposition date: 2013-12-03, release date: 2014-05-14, Last modification date: 2024-10-30)

Primary citation

Blattner, C.,Lee, J.H.,Sliepen, K.,Derking, R.,Falkowska, E.,de la Pena, A.T.,Cupo, A.,Julien, J.P.,van Gils, M.,Lee, P.S.,Peng, W.,Paulson, J.C.,Poignard, P.,Burton, D.R.,Moore, J.P.,Sanders, R.W.,Wilson, I.A.,Ward, A.B.
Structural Delineation of a Quaternary, Cleavage-Dependent Epitope at the gp41-gp120 Interface on Intact HIV-1 Env Trimers.
Immunity, 40:669-680, 2014

PubMed Abstract: All previously characterized broadly neutralizing antibodies to the HIV-1 envelope glycoprotein (Env) target one of four major sites of vulnerability. Here, we define and structurally characterize a unique epitope on Env that is recognized by a recently discovered family of human monoclonal antibodies (PGT151-PGT158). The PGT151 epitope is comprised of residues and glycans at the interface of gp41 and gp120 within a single protomer and glycans from both subunits of a second protomer and represents a neutralizing epitope that is dependent on both gp120 and gp41. Because PGT151 binds only to properly formed, cleaved trimers, this distinctive property, and its ability to stabilize Env trimers, has enabled the successful purification of mature, cleaved Env trimers from the cell surface as a complex with PGT151. Here we compare the structural and functional properties of membrane-extracted Env trimers from several clades with those of the soluble, cleaved SOSIP gp140 trimer.

PubMed: 24768348
DOI: 10.1016/j.immuni.2014.04.008

Experimental method

X-RAY DIFFRACTION (1.8617 Å)