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PDBsum entry 4lsp

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protein ligands metals Protein-protein interface(s) links
Viral protein/immune system PDB id
4lsp

 

 

 

 

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Contents
Protein chains
347 a.a.
216 a.a.
208 a.a.
Ligands
NAG-NAG-BMA
NAG ×12
SO4 ×3
EDO ×11
PEG ×2
Metals
_NA ×3
Waters ×266
PDB id:
4lsp
Name: Viral protein/immune system
Title: Crystal structure of broadly and potently neutralizing antibody vrc- ch31 in complex with HIV-1 clade a/e gp120 93th057
Structure: HIV-1 clade a/e strain 93th057 gp120. Chain: g. Engineered: yes. Heavy chain of antibody vrc-ch31. Chain: h. Engineered: yes. Light chain of antibody vrc-ch31. Chain: l. Engineered: yes
Source: Human immunodeficiency virus 1. Organism_taxid: 11676. Strain: 93th057. Gene: env. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek 293f. Homo sapiens. Organism_taxid: 9606.
Resolution:
2.15Å     R-factor:   0.182     R-free:   0.214
Authors: T.Zhou,S.Moquin,P.D.Kwong
Key ref: T.Zhou et al. (2013). Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies. Immunity, 39, 245-258. PubMed id: 23911655 DOI: 10.1016/j.immuni.2013.04.012
Date:
23-Jul-13     Release date:   04-Sep-13    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q0ED31  (Q0ED31_HV1) -  Envelope glycoprotein gp160 from Human immunodeficiency virus type 1
Seq:
Struc:
 
Seq:
Struc:
857 a.a.
347 a.a.*
Protein chain
No UniProt id for this chain
Struc: 216 a.a.
Protein chain
No UniProt id for this chain
Struc: 208 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1016/j.immuni.2013.04.012 Immunity 39:245-258 (2013)
PubMed id: 23911655  
 
 
Multidonor analysis reveals structural elements, genetic determinants, and maturation pathway for HIV-1 neutralization by VRC01-class antibodies.
T.Zhou, J.Zhu, X.Wu, S.Moquin, B.Zhang, P.Acharya, I.S.Georgiev, H.R.Altae-Tran, G.Y.Chuang, M.G.Joyce, Y.D.Kwon, N.S.Longo, M.K.Louder, T.Luongo, K.McKee, C.A.Schramm, J.Skinner, Y.Yang, Z.Yang, Z.Zhang, A.Zheng, M.Bonsignori, B.F.Haynes, J.F.Scheid, M.C.Nussenzweig, M.Simek, D.R.Burton, W.C.Koff, J.C.Mullikin, M.Connors, L.Shapiro, G.J.Nabel, J.R.Mascola, P.D.Kwong.
 
  ABSTRACT  
 
Antibodies of the VRC01 class neutralize HIV-1, arise in diverse HIV-1-infected donors, and are potential templates for an effective HIV-1 vaccine. However, the stochastic processes that generate repertoires in each individual of >10(12) antibodies make elicitation of specific antibodies uncertain. Here we determine the ontogeny of the VRC01 class by crystallography and next-generation sequencing. Despite antibody-sequence differences exceeding 50%, antibody-gp120 cocrystal structures reveal VRC01-class recognition to be remarkably similar. B cell transcripts indicate that VRC01-class antibodies require few specific genetic elements, suggesting that naive-B cells with VRC01-class features are generated regularly by recombination. Virtually all of these fail to mature, however, with only a few-likely one-ancestor B cell expanding to form a VRC01-class lineage in each donor. Developmental similarities in multiple donors thus reveal the generation of VRC01-class antibodies to be reproducible in principle, thereby providing a framework for attempts to elicit similar antibodies in the general population.
 

 

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