Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2
Article Abstract:
The structure of the tandem Src homology (SH2) domains of SH-protein tyrosine phosphatases (PHP) in complex with monophosphopeptides are analyzed. The two domains, which are stabilized by a disulphide bond and a hydrophobic patch in the interface, can separate the peptide binding sites. Data that shows that peptide orientation and spacing between binding areas is important for enzymatic activation and the defined orientation of the SH2 domains indicate that spatial limits are crucial in the multidomain protein-protein interaction.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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Three-dimensional structure of the tyrosine kinase c-Src
Article Abstract:
The three-dimensional structure of the c-Src tyrosine kinase, which consists of the regulatory and kinase domains and the carboxy-terminal tail, has been determined at 1.7 A resolution. The structure indicates an intramolecular association of the SH2 domain with the phosphorylated Tyr 527. Moreover, the SH3 domain contributes to the closed state stability. Competitive interactions with SH3 and SH2 ligands could lead to the destabilization of the observed conformation.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck
Article Abstract:
The protein p56lck (LCK) Src homology-2 (Lck SH2) was analyzed using crystallographic techniques and found to consist of a complex with an 11-residue phosphopeptide. SH2 domains are modules of approximately 100 amino acid residues contained in many intracellular signal-transduction proteins. Lck SH2's complex features a long peptide/protein interface with 14 hydrogen bonds that resemble other high-affinity protein/protein interactions.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1993
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