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rdf:type |
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lifeskim:mentions |
umls-concept:C0033684,
umls-concept:C0231449,
umls-concept:C0282534,
umls-concept:C0444626,
umls-concept:C0456387,
umls-concept:C0524637,
umls-concept:C1420017,
umls-concept:C1456795,
umls-concept:C1519249,
umls-concept:C1868674,
umls-concept:C2700633
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pubmed:issue |
4
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pubmed:dateCreated |
1999-11-26
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pubmed:databankReference |
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pubmed:abstractText |
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).
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/CD150 antigen,
http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulins,
http://linkedlifedata.com/resource/pubmed/chemical/Intracellular Signaling Peptides...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Library,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphopeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface,
http://linkedlifedata.com/resource/pubmed/chemical/SH2D1A protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SH2D1B protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Transcription Factors
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
4
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
555-61
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pubmed:dateRevised |
2011-9-28
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pubmed:meshHeading |
pubmed-meshheading:10549287-Amino Acid Sequence,
pubmed-meshheading:10549287-Antigens, CD,
pubmed-meshheading:10549287-Binding Sites,
pubmed-meshheading:10549287-Carrier Proteins,
pubmed-meshheading:10549287-Crystallography, X-Ray,
pubmed-meshheading:10549287-Glycoproteins,
pubmed-meshheading:10549287-Humans,
pubmed-meshheading:10549287-Immunoglobulins,
pubmed-meshheading:10549287-Intracellular Signaling Peptides and Proteins,
pubmed-meshheading:10549287-Lymphoproliferative Disorders,
pubmed-meshheading:10549287-Models, Molecular,
pubmed-meshheading:10549287-Molecular Sequence Data,
pubmed-meshheading:10549287-Mutation,
pubmed-meshheading:10549287-Peptide Fragments,
pubmed-meshheading:10549287-Peptide Library,
pubmed-meshheading:10549287-Phosphopeptides,
pubmed-meshheading:10549287-Phosphotyrosine,
pubmed-meshheading:10549287-Protein Binding,
pubmed-meshheading:10549287-Receptors, Cell Surface,
pubmed-meshheading:10549287-Transcription Factors,
pubmed-meshheading:10549287-src Homology Domains
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pubmed:year |
1999
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pubmed:articleTitle |
Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition.
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pubmed:affiliation |
Department of Cancer Biology, Dana-Farber Cancer Institute, Boston, Massachusetts 02115, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, U.S. Gov't, Non-P.H.S.,
Research Support, Non-U.S. Gov't
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