1d4w: Difference between revisions

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[[Image:1d4w.~~gif~~|left|200px]]

[[Image:1d4w.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP IN COMPLEX WITH SLAM PHOSPHOPEPTIDE~~'''~~

===CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP IN COMPLEX WITH SLAM PHOSPHOPEPTIDE===

~~==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).

The line below this paragraph, {{ABSTRACT_PUBMED_10549287}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 10549287 is the PubMed ID number.

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==About this Structure==

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[[Category: Sh2 domain]]

[[Category: Signal transduction]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May 2 13~~:27:27 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:25:34 2008''

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-[[Image:1d4w.gif|left|200px]]
+{{Seed}}
+[[Image:1d4w.png|left|200px]]
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 {{STRUCTURE_1d4w|  PDB=1d4w  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP IN COMPLEX WITH SLAM PHOSPHOPEPTIDE'''
+===CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP IN COMPLEX WITH SLAM PHOSPHOPEPTIDE===
-==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).
+The line below this paragraph, {{ABSTRACT_PUBMED_10549287}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10549287 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10549287}}
 ==About this Structure==
@@ Line 32: / Line 36: @@
 [[Category: Sh2 domain]]
 [[Category: Signal transduction]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 13:27:27 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 22:25:34 2008''