1mq9: Difference between revisions

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==Overview==
==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.
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==
==About this Structure==
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[[Category: Dong, Y.]]
[[Category: Dong, Y.]]
[[Category: Joachimiak, A.]]
[[Category: Joachimiak, A.]]
[[Category: Jun, C.D.]]
[[Category: Jun, C D.]]
[[Category: Liu, J.H.]]
[[Category: Liu, J H.]]
[[Category: McCormack, A.]]
[[Category: McCormack, A.]]
[[Category: Shimaoka, M.]]
[[Category: Shimaoka, M.]]
[[Category: Springer, T.A.]]
[[Category: Springer, T A.]]
[[Category: Takagi, J.]]
[[Category: Takagi, J.]]
[[Category: Wang, J.H.]]
[[Category: Wang, J H.]]
[[Category: Xiao, T.]]
[[Category: Xiao, T.]]
[[Category: Yang, Y.]]
[[Category: Yang, Y.]]
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[[Category: rossmann fold]]
[[Category: rossmann fold]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:25:25 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:53 2008''

Revision as of 14:57, 21 February 2008

File:1mq9.jpg


1mq9, resolution 2.00Å

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Crystal structure of high affinity alphaL I domain with ligand mimetic crystal contact

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 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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