1T0P

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

Summary for 1T0P

• Entry DOI: 10.2210/pdb1t0p/pdb
• Descriptor: Integrin alpha-L, Intercellular adhesion molecule-3, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: rossmann fold; ig-super family domain, immune system
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 29403.53

Authors

Song, G.,Yang, Y.T.,Liu, J.H.,Shimaoko, M.,Springer, T.A.,Wang, J.H. (deposition date: 2004-04-12, release date: 2005-03-08, Last modification date: 2024-11-06)

Primary citation

Song, G.,Yang, Y.,Liu, J.H.,Casasnovas, J.M.,Shimaoka, M.,Springer, T.A.,Wang, J.H.
An atomic resolution view of ICAM recognition in a complex between the binding domains of ICAM-3 and integrin alphaLbeta2.
Proc.Natl.Acad.Sci.Usa, 102:3366-3371, 2005

PubMed Abstract: 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.

PubMed: 15728350
DOI: 10.1073/pnas.0500200102

Experimental method

X-RAY DIFFRACTION (1.66 Å)