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PDBsum entry 2jte

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protein links
Signaling protein PDB id
2jte
Jmol
Contents
Protein chain
64 a.a. *
* Residue conservation analysis
PDB id:
2jte
Name: Signaling protein
Title: Third sh3 domain of cd2ap
Structure: Cd2-associated protein. Chain: a. Fragment: sh3 domain, residues 270-329. Synonym: mesenchyme-to-epithelium transition protein with sh3 domains 1, mets-1. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Gene: cd2ap, mets1. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 20 models
Authors: N.A.J.Van Nuland,R.J.Ortega,M.Romero Romero,E.Ab,A.Ora, M.O.Lopez,A.I.Azuaga
Key ref: J.L.Ortega Roldan et al. (2007). The high resolution NMR structure of the third SH3 domain of CD2AP. J Biomol NMR, 39, 331-336. PubMed id: 17922258
Date:
28-Jul-07     Release date:   11-Dec-07    
PROCHECK
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9JLQ0  (CD2AP_MOUSE) -  CD2-associated protein
Seq:
Struc:
 
Seq:
Struc:
637 a.a.
64 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 3 residue positions (black crosses)

 

 
J Biomol NMR 39:331-336 (2007)
PubMed id: 17922258  
 
 
The high resolution NMR structure of the third SH3 domain of CD2AP.
J.L.Ortega Roldan, M.L.Romero Romero, A.Ora, E.Ab, O.Lopez Mayorga, A.I.Azuaga, N.A.van Nuland.
 
  ABSTRACT  
 
CD2 associated protein (CD2AP) is an adaptor protein that plays an important role in cell to cell union needed for the kidney function. CD2AP interacts, as an adaptor protein, with different natural targets, such as CD2, nefrin, c-Cbl and podocin. These proteins are believed to interact to one of the three SH3 domains that are positioned in the N-terminal region of CD2AP. To understand the network of interactions between the natural targets and the three SH3 domains (SH3-A, B and C), we have started to determine the structures of the individual SH3 domains. Here we present the high-resolution structure of the SH3-C domain derived from NMR data. Full backbone and side-chain assignments were obtained from triple-resonance spectra. The structure was determined from distance restraints derived from high-resolution 600 and 800 MHz NOESY spectra, together with phi and psi torsion angle restraints based on the analysis of 1HN, 15N, 1Halpha, 13Calpha, 13CO and 13Cbeta chemical shifts. Structures were calculated using CYANA and refined in water using RECOORD. The three-dimensional structure of CD2AP SH3-C contains all the features that are typically found in other SH3 domains, including the general binding site for the recognition of polyproline sequences.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19359362 J.L.Ortega-Roldan, M.R.Jensen, B.Brutscher, A.I.Azuaga, M.Blackledge, and N.A.van Nuland (2009).
Accurate characterization of weak macromolecular interactions by titration of NMR residual dipolar couplings: application to the CD2AP SH3-C:ubiquitin complex.
  Nucleic Acids Res, 37, e70.  
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