5eiv

Crystal structure of complex of osteoclast-associated immunoglobulin-like receptor (OSCAR) and a synthetic collagen consensus peptide

spinqualitylabelsall models 5eiv, resolution 2.41Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5eiv is a 11 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ACT, CL, NA, NAG, SO4 NonStd Res: HYP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [OSCAR_HUMAN] Regulator of osteoclastogenesis which plays an important bone-specific function in osteoclast differentiation. Publication Abstract from PubMed The Osteoclast-associated receptor (OSCAR) is a collagen-binding immune receptor with important roles in dendritic cell maturation and activation of inflammatory monocytes as well as in osteoclastogenesis. The crystal structure of the OSCAR ectodomain is presented, both free and in complex with a consensus triple-helical peptide (THP). The structures revealed a collagen-binding site in each Ig-like domain (D1 and D2). The THP binds near a hypothetical collagen-binding groove in D1, but a more extensive interaction with D2 is facilitated by the unusually wide D1-D2 inter-domain angle in OSCAR. Direct binding assays, combined with site-directed mutagenesis, confirm that the primary collagen-binding site in OSCAR resides in D2, in marked contrast to the related collagen receptors, GPVI and LAIR-1. Monomeric OSCAR D1D2 binds to the consensus THP with a KD of 28 muM measured in solution, but shows a higher affinity (KD 1.5 muM) when binding to a solid-phase THP, most likely due to an avidity effect. These data suggest a two-stage model for the interaction of OSCAR with a collagen fibril, with transient, low-affinity interactions initiated by the membrane-distal D1, followed by firm adhesion to the primary binding site in D2. Structural basis for collagen recognition by the immune receptor OSCAR.,Zhou L, Hinerman JM, Blaszczyk M, Miller JL, Conrady DG, Barrow AD, Chirgadze DY, Bihan D, Farndale RW, Herr AB Blood. 2015 Nov 9. pii: blood-2015-08-667055. PMID:26552697 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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