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PDBsum entry 1wbr

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protein links
Immunoglobulin fold PDB id
1wbr
Jmol
Contents
Protein chain
19 a.a.
PDB id:
1wbr
Name: Immunoglobulin fold
Title: Solution structure of the human cd4 (403-419) receptor peptide, nmr, 32 structures
Structure: Cd4 receptor. Chain: a. Fragment: 403 - 419. Synonym: cd4, 403- 419. Engineered: yes. Mutation: yes. Other_details: chemically synthesized
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 32 models
Authors: D.Willbold,P.Roesch
Key ref: D.Willbold and P.Rösch (1996). Solution Structure of the Human CD4 (403-419) Receptor Peptide. J Biomed Sci, 3, 435-441. PubMed id: 11725124
Date:
20-Dec-96     Release date:   12-Mar-97    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P01730  (CD4_HUMAN) -  T-cell surface glycoprotein CD4
Seq:
Struc:
458 a.a.
18 a.a.*
Key:    PfamA domain  Secondary structure
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
J Biomed Sci 3:435-441 (1996)
PubMed id: 11725124  
 
 
Solution Structure of the Human CD4 (403-419) Receptor Peptide.
D.Willbold, P.Rösch.
 
  ABSTRACT  
 
The cytoplasmic part of CD4 is known to be essential for the interaction with the human immunodeficiency virus type 1 proteins Vpu and Nef. The 17 amino acid synthetic peptide CD4 (403-419) with the amino acid sequence of the membrane proximal part of the cytoplasmic domain of the human CD4 receptor was structurally investigated by circular dichroism and nuclear magnetic resonance spectroscopy. The average alpha-helical content of the peptide could be estimated to be around 25%. Chemical shift index analysis and the connectivity pattern in nuclear Overhauser enhancement spectra located the alpha-helical part of the peptide from Gln403 to Arg412. It may be speculated that this amphipathic alpha-helix is the contact region with the Vpu and Nef proteins. Copyright 1996 S. Karger AG, Basel
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
15976924 L.Briese, A.Preusser, and D.Willbold (2005).
Mapping the binding site of full length HIV-1 Nef on human Lck SH3 by NMR spectroscopy.
  J Biomed Sci, 12, 451-456.  
11264384 A.Preusser, L.Briese, A.S.Baur, and D.Willbold (2001).
Direct in vitro binding of full-length human immunodeficiency virus type 1 Nef protein to CD4 cytoplasmic domain.
  J Virol, 75, 3960-3964.  
9182993 D.Willbold, S.Hoffmann, and P.Rösch (1997).
Secondary structure and tertiary fold of the human immunodeficiency virus protein U (Vpu) cytoplasmic domain in solution.
  Eur J Biochem, 245, 581-588.
PDB code: 1vpu
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