Much more than the sum of the parts: structures of the dual SH2 domains of ZAP-70 and Syp.
Proteins involved in signaling pathways frequently contain one or more SH2 domains. New structural information on proteins that carry two SH2 domains show, surprisingly, that the domains are closely interlinked, so the binding sites are rigidly oriented with respect to each other. Thus, only ligands with the right spacing of the phosphotyrosines will be tightly bound.
Cowburn
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The Rockefeller University, 1230 York Avenue, New York, NY, 10021, USA.
D047908:Intracellular Signaling Peptides and Proteins; D011487:Protein Conformation; D054592:Protein Tyrosine Phosphatase, Non-Receptor Type 11; D053824:Protein Tyrosine Phosphatase, Non-Receptor Type 6; D017027:Protein Tyrosine Phosphatases / Q000737:chemistry*; D011505:Protein-Tyrosine Kinases / Q000737:chemistry*; D054593:SH2 Domain-Containing Protein Tyrosine Phosphatases; D051746:ZAP-70 Protein-Tyrosine Kinase; D018909:src Homology Domains
D047908:Intracellular Signaling Peptides and Proteins; D011505:Protein-Tyrosine Kinases; D051746:ZAP-70 Protein-Tyrosine Kinase; D054592:Protein Tyrosine Phosphatase, Non-Receptor Type 11; D053824:Protein Tyrosine Phosphatase, Non-Receptor Type 6; D017027:Protein Tyrosine Phosphatases; D054593:SH2 Domain-Containing Protein Tyrosine Phosphatases