1mqa
From Proteopedia
OCA (Talk | contribs)
(New page: 200px<br /> <applet load="1mqa" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mqa, resolution 2.50Å" /> '''Crystal structure o...)
Next diff →
Revision as of 16:07, 12 November 2007
|
Crystal structure of high affinity alphaL I domain in the absence of ligand or metal
Overview
The structure of the I domain of integrin alpha L beta 2 bound to the Ig, superfamily ligand ICAM-1 reveals the open ligand binding conformation and, the first example of an integrin-IgSF interface. The I domain Mg2+, directly coordinates Glu-34 of ICAM-1, and a dramatic swing of I domain, residue Glu-241 enables a critical salt bridge. Liganded and unliganded, structures for both high- and intermediate-affinity mutant I domains, reveal that ligand binding can induce conformational change in the alpha L, I domain and that allosteric signals can convert the closed conformation, to intermediate or open conformations without ligand binding. Pulling down, on the C-terminal alpha 7 helix with introduced disulfide bonds ratchets, the beta 6-alpha 7 loop into three different positions in the closed, intermediate, and open conformations, with a progressive increase in, affinity.
About this Structure
1MQA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structures of the alpha L I domain and its complex with ICAM-1 reveal a shape-shifting pathway for integrin regulation., Shimaoka M, Xiao T, Liu JH, Yang Y, Dong Y, Jun CD, McCormack A, Zhang R, Joachimiak A, Takagi J, Wang JH, Springer TA, Cell. 2003 Jan 10;112(1):99-111. PMID:12526797
Page seeded by OCA on Mon Nov 12 18:14:07 2007
