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PDBsum entry 4jm4
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protein Protein-protein interface(s) links
Immune system PDB id
4jm4

 

 

 

 

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Contents
Protein chains
229 a.a.
214 a.a.
Waters ×273
PDB id:
4jm4
Name: Immune system
Title: Crystal structure of pgt 135 fab
Structure: Pgt 135 heavy chain. Chain: h. Fragment: fab. Engineered: yes. Pgt 135 light chain. Chain: l. Fragment: fab. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: spodoptera frugiperda. Expression_system_taxid: 7108. Expression_system_taxid: 7108
Resolution:
1.75Å     R-factor:   0.209     R-free:   0.245
Authors: L.Kong,I.A.Wilson
Key ref: L.Kong et al. (2013). Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120. Nat Struct Biol, 20, 796-803. PubMed id: 23708606 DOI: 10.1038/nsmb.2594
Date:
13-Mar-13     Release date:   29-May-13    
PROCHECK
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 Headers
 References

Protein chain
No UniProt id for this chain
Struc: 229 a.a.
Protein chain
No UniProt id for this chain
Struc: 214 a.a.
Key:    Secondary structure  CATH domain

 

 
DOI no: 10.1038/nsmb.2594 Nat Struct Biol 20:796-803 (2013)
PubMed id: 23708606  
 
 
Supersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120.
L.Kong, J.H.Lee, K.J.Doores, C.D.Murin, J.P.Julien, R.McBride, Y.Liu, A.Marozsan, A.Cupo, P.J.Klasse, S.Hoffenberg, M.Caulfield, C.R.King, Y.Hua, K.M.Le, R.Khayat, M.C.Deller, T.Clayton, H.Tien, T.Feizi, R.W.Sanders, J.C.Paulson, J.P.Moore, R.L.Stanfield, D.R.Burton, A.B.Ward, I.A.Wilson.
 
  ABSTRACT  
 
A substantial proportion of the broadly neutralizing antibodies (bnAbs) identified in certain HIV-infected donors recognize glycan-dependent epitopes on HIV-1 gp120. Here we elucidate how the bnAb PGT 135 binds its Asn332 glycan-dependent epitope from its 3.1-Å crystal structure with gp120, CD4 and Fab 17b. PGT 135 interacts with glycans at Asn332, Asn392 and Asn386, using long CDR loops H1 and H3 to penetrate the glycan shield and access the gp120 protein surface. EM reveals that PGT 135 can accommodate the conformational and chemical diversity of gp120 glycans by altering its angle of engagement. Combined structural studies of PGT 135, PGT 128 and 2G12 show that this Asn332-dependent antigenic region is highly accessible and much more extensive than initially appreciated, which allows for multiple binding modes and varied angles of approach; thereby it represents a supersite of vulnerability for antibody neutralization.
 

 

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