This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1r1q

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1r1q.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1r1q.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1r1q| PDB=1r1q | SCENE= }}
{{STRUCTURE_1r1q| PDB=1r1q | SCENE= }}
-
'''Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads'''
+
===Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads===
-
==Overview==
+
<!--
-
The transmembrane protein, linker for activation of T cells (LAT), is essential for T-cell activation and development. Phosphorylation of LAT at multiple tyrosines creates binding sites for the adaptors Gads and Grb2, leading to nucleation of multiprotein signaling complexes. Human LAT contains five potential binding sites for Gads, of which only those at Tyr171 and Tyr191 appear necessary for T-cell function. We asked whether Gads binds preferentially to these sites, as differential recognition could assist in assembling defined LAT-based complexes. Measured calorimetrically, Gads-SH2 binds LAT tyrosine phosphorylation sites 171 and 191 with higher affinities than the other sites, with the differences ranging from only several fold weaker binding to no detectable interaction. Crystal structures of Gads-SH2 complexed with phosphopeptides representing sites 171, 191 and 226 were determined to 1.8-1.9 A resolutions. The structures reveal the basis for preferential recognition of specific LAT sites by Gads, as well as for the relatively greater promiscuity of the related adaptor Grb2, whose binding also requires asparagine at position +2 C-terminal to the phosphorylated tyrosine.
+
The line below this paragraph, {{ABSTRACT_PUBMED_15029250}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 15029250 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_15029250}}
==About this Structure==
==About this Structure==
Line 28: Line 32:
[[Category: Phosphopeptide]]
[[Category: Phosphopeptide]]
[[Category: Sh2]]
[[Category: Sh2]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:58:09 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 10:45:38 2008''

Revision as of 07:46, 29 July 2008

Image:1r1q.png

Template:STRUCTURE 1r1q

Structural Basis for Differential Recognition of Tyrosine Phosphorylated Sites in the Linker for Activation of T cells (LAT) by the Adaptor Protein Gads

Template:ABSTRACT PUBMED 15029250

About this Structure

1R1Q is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Structural basis for differential recognition of tyrosine-phosphorylated sites in the linker for activation of T cells (LAT) by the adaptor Gads., Cho S, Velikovsky CA, Swaminathan CP, Houtman JC, Samelson LE, Mariuzza RA, EMBO J. 2004 Apr 7;23(7):1441-51. Epub 2004 Mar 18. PMID:15029250

Page seeded by OCA on Tue Jul 29 10:45:38 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1r1q"
Personal tools