1d4t: Difference between revisions

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New page: left|200px<br /> <applet load="1d4t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d4t, resolution 1.10Å" /> '''CRYSTAL STRUCTURE O...
 
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[[Image:1d4t.gif|left|200px]]<br />
[[Image:1d4t.gif|left|200px]]<br /><applet load="1d4t" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1d4t" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1d4t, resolution 1.10&Aring;" />
caption="1d4t, resolution 1.10&Aring;" />
'''CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP IN COMPLEX WITH A SLAM PEPTIDE'''<br />
'''CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP IN COMPLEX WITH A SLAM PEPTIDE'''<br />


==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).


==Disease==
==Disease==
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==About this Structure==
==About this Structure==
1D4T is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D4T OCA].  
1D4T is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D4T OCA].  


==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Eck, M.J.]]
[[Category: Eck, M J.]]
[[Category: Poy, F.]]
[[Category: Poy, F.]]
[[Category: Saxena, K.]]
[[Category: Saxena, K.]]
[[Category: Sayos, J.]]
[[Category: Sayos, J.]]
[[Category: Yaffe, M.B.]]
[[Category: Yaffe, M B.]]
[[Category: peptide recognition]]
[[Category: peptide recognition]]
[[Category: sh2 domain]]
[[Category: sh2 domain]]
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[[Category: tyrosine kinase]]
[[Category: tyrosine kinase]]


''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:28:46 2007''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:00 2008''