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Localisation of the C1q binding site within C 1 q receptor/calreticulin
Author(s) -
Stuart G.R.,
Lynch N.J.,
Lu J.,
Geick A.,
Moffatt B.E.,
Sim R.B.,
Schwaeble W.J.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01156-8
Subject(s) - calreticulin , collectin , binding site , receptor , microbiology and biotechnology , recombinant dna , biology , plasma protein binding , chemistry , biochemistry , endoplasmic reticulum , innate immune system , gene
Clq receptor (C1gR/collectin receptor) is located on many cell types. Binding of C1q to these cells elicits numerous responses. Protein sequencing has shown that C1gR is almost identical to calreticulin (CaR), an abundant multifunctional protein. Radioiodinated C1gR and CaR bind to C1q with identical characteristics. Three recombinant C1gR/CaR domains (N‐, C‐terminal domains and central P‐domain) were expressed using the Thiofusion system, and used to study the interaction with C1q. Both the N‐ and P‐domains were implicated in C1q binding. A region, termed the S‐domain, spanning the N and P intersection was expressed, and showed concentration‐dependent binding to C1q, demonstrating that the Clq binding site lies within this region.