1mq9
Crystal structure of high affinity alphaL I domain with ligand mimetic crystal contact
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OverviewOverview
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 StructureAbout this Structure
1MQ9 is a Single protein structure of sequence from Homo sapiens with MN as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
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