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1D1Z

CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP

Summary for 1D1Z
Entry DOI10.2210/pdb1d1z/pdb
Related1D4T 1D4W
DescriptorSAP SH2 DOMAIN, SULFATE ION (3 entities in total)
Functional Keywordssh2 domains, gene regulation
Biological sourceHomo sapiens (human)
Cellular locationCytoplasm : O60880
Total number of polymer chains4
Total formula weight47482.01
Authors
Poy, F.,Yaffe, M.B.,Sayos, J.,Saxena, K.,Eck, M.J. (deposition date: 1999-09-22, release date: 1999-10-13, Last modification date: 2024-02-07)
Primary citationPoy, F.,Yaffe, M.B.,Sayos, J.,Saxena, K.,Morra, M.,Sumegi, J.,Cantley, L.C.,Terhorst, C.,Eck, M.J.
Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition.
Mol.Cell, 4:555-561, 1999
Cited by
PubMed Abstract: SAP, the product of the gene mutated in X-linked lymphoproliferative syndrome (XLP), consists of a single SH2 domain that has been shown to bind the cytoplasmic tail of the lymphocyte coreceptor SLAM. Here we describe structures that show that SAP binds phosphorylated and nonphosphorylated SLAM peptides in a similar mode, with the tyrosine or phosphotyrosine residue inserted into the phosphotyrosine-binding pocket. We find that specific interactions with residues N-terminal to the tyrosine, in addition to more characteristic C-terminal interactions, stabilize the complexes. A phosphopeptide library screen and analysis of mutations identified in XLP patients confirm that these extended interactions are required for SAP function. Further, we show that SAP and the similar protein EAT-2 recognize the sequence motif TIpYXX(V/I).
PubMed: 10549287
DOI: 10.1016/S1097-2765(00)80206-3
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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