Abstract:
:Leukocyte-associated immunoglobulin-like receptor-1 (LAIR-1), one of the most widely spread immune receptors, attenuates immune cell activation when bound to specific sites in collagen. The collagen-binding domain of LAIR-1 is homologous to that of glycoprotein VI (GPVI), a collagen receptor crucial for platelet activation. Because LAIR-1 and GPVI also display overlapping collagen-binding specificities, a common structural basis for collagen recognition would appear likely. Therefore, it is crucial to gain insight into the molecular interaction of both receptors with their ligand to prevent unwanted cross-reactions during therapeutic intervention. We determined the crystal structure of LAIR-1 and mapped its collagen-binding site by nuclear magnetic resonance (NMR) titrations and mutagenesis. Our data identify R59, E61, and W109 as key residues for collagen interaction. These residues are strictly conserved in LAIR-1 and GPVI alike; however, they are located outside the previously proposed GPVI collagen-binding site. Our data provide evidence for an unanticipated mechanism of collagen recognition common to LAIR-1 and GPVI. This fundamental insight will contribute to the exploration of specific means of intervention in collagen-induced signaling in immunity and hemostasis.
journal_name
Bloodjournal_title
Bloodauthors
Brondijk TH,de Ruiter T,Ballering J,Wienk H,Lebbink RJ,van Ingen H,Boelens R,Farndale RW,Meyaard L,Huizinga EGdoi
10.1182/blood-2009-10-246322subject
Has Abstractpub_date
2010-02-18 00:00:00pages
1364-73issue
7eissn
0006-4971issn
1528-0020pii
blood-2009-10-246322journal_volume
115pub_type
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