spacer
spacer

PDBsum entry 1tce
Go to PDB code: 
protein Protein-protein interface(s) links
Complex (signal transduction/peptide) PDB id
1tce

 

 

 

 

Loading ...

 
JSmol PyMol  
Contents
Protein chains
107 a.a. *
14 a.a. *
* Residue conservation analysis
PDB id:
1tce
Name: Complex (signal transduction/peptide)
Title: Solution nmr structure of the shc sh2 domain complexed with a tyrosine-phosphorylated peptide from the t-cell receptor, minimized average structure
Structure: Shc. Chain: a. Fragment: sh2 domain. Engineered: yes. Phosphopeptide of the zeta chain of t cell receptor. Chain: b. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Strain: bl21 (de3). Cell_line: bl21. Gene: sh2 domain of shc. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 1 models
Authors: M.-M.Zhou,R.P.Meadows,T.M.Logan,H.S.Yoon,W.R.Wade,K.S.Ravichandran, S.J.Burakoff,S.W.Feisk
Key ref: M.M.Zhou et al. (1995). Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor. Proc Natl Acad Sci U S A, 92, 7784-7788. PubMed id: 7544002 DOI: 10.1073/pnas.92.17.7784
Date:
27-Mar-96     Release date:   15-May-97    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P29353  (SHC1_HUMAN) -  SHC-transforming protein 1 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		583 a.a.
107 a.a.*
Protein chain
Pfam   ArchSchema ?
P20963  (CD3Z_HUMAN) -  T-cell surface glycoprotein CD3 zeta chain from Homo sapiens
Seq:
Struc: 		164 a.a.
14 a.a.
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

 

 
DOI no: 10.1073/pnas.92.17.7784 Proc Natl Acad Sci U S A 92:7784-7788 (1995)
PubMed id: 7544002  
 
 
Solution structure of the Shc SH2 domain complexed with a tyrosine-phosphorylated peptide from the T-cell receptor.
M.M.Zhou, R.P.Meadows, T.M.Logan, H.S.Yoon, W.S.Wade, K.S.Ravichandran, S.J.Burakoff, S.W.Fesik.
 
  ABSTRACT  
 
She is a widely expressed adapter protein that plays an important role in signaling via a variety of cell surface receptors and has been implicated in coupling the stimulation of growth factor, cytokine, and antigen receptors to the Ras signaling pathway. She interacts with several tyrosine-phosphorylated receptors through its C-terminal SH2 domain, and one of the mechanisms of T-cell receptor-mediated Ras activation involves the interaction of the Shc SH2 domain with the tyrosine-phosphorylated zeta chain of the T-cell receptor. Here we describe a high-resolution NMR structure of the Shc SH2 domain complexed to a phosphopeptide (GHDGLpYQGLSTATK) corresponding to a portion of the zeta chain of the T-cell receptor. Although the overall architecture of the protein is similar to other SH2 domains, distinct structural differences were observed in the smaller beta-sheet, BG loop, (pY + 3) phosphopeptide-binding site, and relative position of the bound phosphopeptide.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19289054 A.Suenaga, M.Hatakeyama, A.B.Kiyatkin, R.Radhakrishnan, M.Taiji, and B.N.Kholodenko (2009).
Molecular dynamics simulations reveal that Tyr-317 phosphorylation reduces Shc binding affinity for phosphotyrosyl residues of epidermal growth factor receptor.
  Biophys J, 96, 2278-2288.  
19909360 F.Finetti, M.T.Savino, and C.T.Baldari (2009).
Positive and negative regulation of antigen receptor signaling by the Shc family of protein adapters.
  Immunol Rev, 232, 115-134.  
19226165 W.J.Choi, S.E.Kim, A.G.Stephen, I.Weidlich, A.Giubellino, F.Liu, K.M.Worthy, L.Bindu, M.J.Fivash, M.C.Nicklaus, D.P.Bottaro, R.J.Fisher, and T.R.Burke (2009).
Identification of Shc Src homology 2 domain-binding peptoid-peptide hybrids.
  J Med Chem, 52, 1612-1618.  
17894853 C.J.Porter, J.M.Matthews, J.P.Mackay, S.E.Pursglove, J.W.Schmidberger, P.J.Leedman, S.C.Pero, D.N.Krag, M.C.Wilce, and J.A.Wilce (2007).
Grb7 SH2 domain structure and interactions with a cyclic peptide inhibitor of cancer cell migration and proliferation.
  BMC Struct Biol, 7, 58.
PDB code: 2qms
12577262 J.B.Mitchell, and J.Smith (2003).
D-amino acid residues in peptides and proteins.
  Proteins, 50, 563-571.  
12614360 L.Zhang, U.Lorenz, and K.S.Ravichandran (2003).
Role of Shc in T-cell development and function.
  Immunol Rev, 191, 183-195.  
10662684 J.E.Ladbury, and S.Arold (2000).
Searching for specificity in SH domains.
  Chem Biol, 7, R3-R8.  
10502299 Y.Xu, and G.Carpenter (1999).
Identification of cadherin tyrosine residues that are phosphorylated and mediate Shc association.
  J Cell Biochem, 75, 264-271.  
9241420 J.Kuriyan, and D.Cowburn (1997).
Modular peptide recognition domains in eukaryotic signaling.
  Annu Rev Biophys Biomol Struct, 26, 259-288.  
  9271429 K.S.Ravichandran, M.M.Zhou, J.C.Pratt, J.E.Harlan, S.F.Walk, S.W.Fesik, and S.J.Burakoff (1997).
Evidence for a requirement for both phospholipid and phosphotyrosine binding via the Shc phosphotyrosine-binding domain in vivo.
  Mol Cell Biol, 17, 5540-5549.  
9351806 T.D.Mulhern, G.L.Shaw, C.J.Morton, A.J.Day, and I.D.Campbell (1997).
The SH2 domain from the tyrosine kinase Fyn in complex with a phosphotyrosyl peptide reveals insights into domain stability and binding specificity.
  Structure, 5, 1313-1323.
PDB codes: 1aot 1aou
8768898 A.J.Wand, and S.W.Englander (1996).
Protein complexes studied by NMR spectroscopy.
  Curr Opin Biotechnol, 7, 403-408.  
8610109 J.P.O'Bryan, Z.Songyang, L.Cantley, C.J.Der, and T.Pawson (1996).
A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain.
  Proc Natl Acad Sci U S A, 93, 2729-2734.  
8794768 K.H.Thornton, W.T.Mueller, P.McConnell, G.Zhu, A.R.Saltiel, and V.Thanabal (1996).
Nuclear magnetic resonance solution structure of the growth factor receptor-bound protein 2 Src homology 2 domain.
  Biochemistry, 35, 11852-11864.
PDB code: 1ghu
8643566 K.S.Ravichandran, V.Igras, S.E.Shoelson, S.W.Fesik, and S.J.Burakoff (1996).
Evidence for a role for the phosphotyrosine-binding domain of Shc in interleukin 2 signaling.
  Proc Natl Acad Sci U S A, 93, 5275-5280.  
8599763 R.T.Nolte, M.J.Eck, J.Schlessinger, S.E.Shoelson, and S.C.Harrison (1996).
Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes.
  Nat Struct Biol, 3, 364-374.
PDB codes: 2iug 2iuh 2iui
  8868476 S.Réty, K.Fütterer, R.A.Grucza, C.M.Munoz, W.A.Frazier, and G.Waksman (1996).
pH-Dependent self-association of the Src homology 2 (SH2) domain of the Src homologous and collagen-like (SHC) protein.
  Protein Sci, 5, 405-413.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.

 

spacer
spacer