PDBsum entry 4nug

Immune system

PDB id: 4nug

Contents

Protein chains

218 a.a.

236 a.a.

Ligands

P6G ×2

Waters ×485

PDB id:

4nug

Name:

Immune system

Title:

Crystal structure of HIV-1 broadly neutralizing antibody pgt151

Structure:

Pgt151 light chain. Chain: l. Engineered: yes. Pgt151 heavy chain. Chain: h. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek 293f. Expression_system_cell_line: hek 293f

Resolution:

1.86Å R-factor: 0.161 R-free: 0.207

Authors:

C.Blattner,I.A.Wilson

Key ref:

C.Blattner et al. (2014). Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity, 40, 669-680. PubMed id: 24768348 DOI: 10.1016/j.immuni.2014.04.008

Date:

03-Dec-13 Release date: 14-May-14

Protein chain

Q8TCD0  (Q8TCD0_HUMAN) -  Ig-like domain-containing protein from Homo sapiens

Seq: 239 a.a.

Struc: 218 a.a.*

Protein chain

S6BAM6  (S6BAM6_HUMAN) -  IgG H chain from Homo sapiens

Seq: 319 a.a.

Struc: 236 a.a.*

* PDB and UniProt seqs differ at 107 residue positions (black crosses)

DOI no: 10.1016/j.immuni.2014.04.008

Immunity 40:669-680 (2014)

PubMed id: 24768348

Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers.

C.Blattner, J.H.Lee, K.Sliepen, R.Derking, E.Falkowska, A.T.de la Peña, A.Cupo, J.P.Julien, M.van Gils, P.S.Lee, W.Peng, J.C.Paulson, P.Poignard, D.R.Burton, J.P.Moore, R.W.Sanders, I.A.Wilson, A.B.Ward.

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.