1d1z

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1d1z.gif|left|200px]]
[[Image:1d1z.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1d1z |SIZE=350|CAPTION= <scene name='initialview01'>1d1z</scene>, resolution 1.4&Aring;
+
The line below this paragraph, containing "STRUCTURE_1d1z", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1d1z| PDB=1d1z | SCENE= }}
-
|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>
+
-
}}
+
'''CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP'''
'''CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP'''
Line 30: Line 27:
[[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 Fri May 2 13:21:37 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:33:06 2008''
+

Revision as of 10:21, 2 May 2008

Template:STRUCTURE 1d1z

CRYSTAL STRUCTURE OF THE XLP PROTEIN SAP


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).

About this Structure

1D1Z is a Single protein structure of sequence from Homo sapiens. 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 Page seeded by OCA on Fri May 2 13:21:37 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools