1t0p

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(New page: 200px<br /> <applet load="1t0p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0p, resolution 1.66&Aring;" /> '''Structural Basis of...)
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<applet load="1t0p" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1t0p, resolution 1.66&Aring;" />
caption="1t0p, resolution 1.66&Aring;" />
'''Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A'''<br />
'''Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A'''<br />
==Overview==
==Overview==
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Within the Ig superfamily (IgSF), intercellular adhesion molecules (ICAMs), form a subfamily that binds the leukocyte integrin alphaLbeta2. We report, a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1), in complex with the inserted domain, the ligand-binding domain of, alphaLbeta2. This high-resolution structure and comparisons among ICAM, subfamily members establish that the binding of ICAM-3 D1 onto the, inserted domain represents a common docking mode for ICAM subfamily, members. The markedly different off-rates of ICAM-1, -2, and -3 appear to, be determined by the hydrophobicity of residues that surround a metal, coordination bond in the alphaLbeta2-binding interfaces. Variation in, composition of glycans on the periphery of the interfaces influences, on-rate.
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Within the Ig superfamily (IgSF), intercellular adhesion molecules (ICAMs) form a subfamily that binds the leukocyte integrin alphaLbeta2. We report a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1) in complex with the inserted domain, the ligand-binding domain of alphaLbeta2. This high-resolution structure and comparisons among ICAM subfamily members establish that the binding of ICAM-3 D1 onto the inserted domain represents a common docking mode for ICAM subfamily members. The markedly different off-rates of ICAM-1, -2, and -3 appear to be determined by the hydrophobicity of residues that surround a metal coordination bond in the alphaLbeta2-binding interfaces. Variation in composition of glycans on the periphery of the interfaces influences on-rate.
==About this Structure==
==About this Structure==
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1T0P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and MG as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1T0P OCA].
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1T0P is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0P OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Liu, J.H.]]
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[[Category: Liu, J H.]]
[[Category: Shimaoko, M.]]
[[Category: Shimaoko, M.]]
[[Category: Song, G.]]
[[Category: Song, G.]]
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[[Category: Springer, T.A.]]
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[[Category: Springer, T A.]]
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[[Category: Wang, J.H.]]
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[[Category: Wang, J H.]]
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[[Category: Yang, Y.T.]]
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[[Category: Yang, Y T.]]
[[Category: MG]]
[[Category: MG]]
[[Category: NAG]]
[[Category: NAG]]
[[Category: rossmann fold; ig-super family domain]]
[[Category: rossmann fold; ig-super family domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:18:52 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:34 2008''

Revision as of 13:08, 21 February 2008


1t0p, resolution 1.66Å

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Structural Basis of ICAM recognition by integrin alpahLbeta2 revealed in the complex structure of binding domains of ICAM-3 and alphaLbeta2 at 1.65 A

Overview

Within the Ig superfamily (IgSF), intercellular adhesion molecules (ICAMs) form a subfamily that binds the leukocyte integrin alphaLbeta2. We report a 1.65-A-resolution crystal structure of the ICAM-3 N-terminal domain (D1) in complex with the inserted domain, the ligand-binding domain of alphaLbeta2. This high-resolution structure and comparisons among ICAM subfamily members establish that the binding of ICAM-3 D1 onto the inserted domain represents a common docking mode for ICAM subfamily members. The markedly different off-rates of ICAM-1, -2, and -3 appear to be determined by the hydrophobicity of residues that surround a metal coordination bond in the alphaLbeta2-binding interfaces. Variation in composition of glycans on the periphery of the interfaces influences on-rate.

About this Structure

1T0P is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2., Song G, Yang Y, Liu JH, Casasnovas JM, Shimaoka M, Springer TA, Wang JH, Proc Natl Acad Sci U S A. 2005 Mar 1;102(9):3366-71. Epub 2005 Feb 22. PMID:15728350

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