1d1z

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(New page: 200px<br /> <applet load="1d1z" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d1z, resolution 1.4&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1d1z.gif|left|200px]]<br />
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[[Image:1d1z.gif|left|200px]]<br /><applet load="1d1z" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1d1z" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1d1z, resolution 1.4&Aring;" />
caption="1d1z, resolution 1.4&Aring;" />
'''CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP'''<br />
'''CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP'''<br />
==Overview==
==Overview==
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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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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==
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1D1Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D1Z OCA].
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1D1Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D1Z OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Eck, M.J.]]
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[[Category: Eck, M J.]]
[[Category: Poy, F.]]
[[Category: Poy, F.]]
[[Category: Saxena, K.]]
[[Category: Saxena, K.]]
[[Category: Sayos, J.]]
[[Category: Sayos, J.]]
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[[Category: Yaffe, M.B.]]
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[[Category: Yaffe, M B.]]
[[Category: SO4]]
[[Category: SO4]]
[[Category: sh2 domains]]
[[Category: sh2 domains]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:27:43 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:18 2008''

Revision as of 10:12, 21 February 2008

Image:1d1z.gif

1d1z, resolution 1.4Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP

Contents

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).

Disease

Known diseases associated with this structure: Amyloidosis, secondary, susceptibility to OMIM:[104770], Lymphoproliferative syndrome, X-linked OMIM:[300490]

About this Structure

1D1Z is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structures of the XLP protein SAP reveal a class of SH2 domains with extended, phosphotyrosine-independent sequence recognition., Poy F, Yaffe MB, Sayos J, Saxena K, Morra M, Sumegi J, Cantley LC, Terhorst C, Eck MJ, Mol Cell. 1999 Oct;4(4):555-61. PMID:10549287

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