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.
journal_name
Proc Natl Acad Sci U S Aauthors
Song G,Yang Y,Liu JH,Casasnovas JM,Shimaoka M,Springer TA,Wang JHdoi
10.1073/pnas.0500200102keywords:
subject
Has Abstractpub_date
2005-03-01 00:00:00pages
3366-71issue
9eissn
0027-8424issn
1091-6490pii
0500200102journal_volume
102pub_type
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