› 1tce

Solution NMR

SOLUTION NMR STRUCTURE OF THE SHC SH2 DOMAIN COMPLEXED WITH A TYROSINE-PHOSPHORYLATED PEPTIDE FROM THE T-CELL RECEPTOR, MINIMIZED AVERAGE STRUCTURE

Released:
DOI: 10.2210/pdb1tce/pdb
PDB 1tce coloured by chain and viewed from the front.
PDB 1tce coloured by chain and viewed from the side.
PDB 1tce coloured by chain and viewed from the top.
Source organism: Homo sapiens
Primary publication:
Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor.
Zhou MM, Meadows RP, Logan TM, Yoon HS, Wade WS, Ravichandran KS, Burakoff SJ, Fesik SW
Proc. Natl. Acad. Sci. U.S.A. 92 7784-8 (1995)
PMID: 7544002

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
SHC-transforming protein 1 Chain: A
Molecule details ›
Chain: A
Length: 107 amino acids
Theoretical weight: 12.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29353 (Residues: 480-583; Coverage: 18%)
Gene names: SHC, SHC1, SHCA
Structure domains: SH2 domain
T-cell surface glycoprotein CD3 zeta chain Chain: B
Molecule details ›
Chain: B
Length: 14 amino acids
Theoretical weight: 1.53 KDa
Source organism: Homo sapiens
Expression system: Not provided
UniProt:
  • Canonical: P20963 (Residues: 137-150; Coverage: 10%)
Gene names: CD247, CD3Z, T3Z, TCRZ

Ligands and Environments

No bound ligands
1 modified residue:
Ligand PTR 1 x PTR

Experiments and Validation Details

Entry percentile scores
Expression systems:
  • Escherichia coli
  • Not provided

Quick links

Citations

10 review citations

Crammed signaling motifs in the T-cell receptor.
Borroto et al. (2014)
9 more

5 mentions without citation

Computational Prediction of MoRFs, Short Disorder-to-order Transitioning Protein Binding Regions.
Katuwawala et al. (2019)
4 more