1d1z: Difference between revisions
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|PDB= 1d1z |SIZE=350|CAPTION= <scene name='initialview01'>1d1z</scene>, resolution 1.4Å | |PDB= 1d1z |SIZE=350|CAPTION= <scene name='initialview01'>1d1z</scene>, resolution 1.4Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1d4w|1D4W]], [[1d4t|1D4T]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1d1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1d1z OCA], [http://www.ebi.ac.uk/pdbsum/1d1z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1d1z RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==Overview== | ||
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). | 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). | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Sayos, J.]] | [[Category: Sayos, J.]] | ||
[[Category: Yaffe, M B.]] | [[Category: Yaffe, M B.]] | ||
[[Category: sh2 domain]] | [[Category: sh2 domain]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:33:06 2008'' | ||