Abstract:
:A recombinant peptide encoding the CD11b A domain bound 54Mn2+ with a high affinity. Other divalent cations, including Mg2+, Zn2+, Ni2+, Co2+, and Cd2+, but not Ca2+ or Ba2+, competed effectively for Mn2+ binding. Amino acid substitutions within two conserved and noncontiguous regions in the recombinant peptide abolished 54Mn2+ binding. When these substitutions were introduced independently in complement receptor type 3 (CR3), each abolished the metal-dependent binding of the receptor to the major C3 opsonin iC3b, without impairing subunit association or surface expression of the receptor. These findings identify an unsuspected and novel metal-binding site within the A domain of CR3 that is required for metal-dependent ligand binding and also identify a good target for designing drugs aimed at countering the inflammatory potential of this key receptor.
journal_name
Celljournal_title
Cellauthors
Michishita M,Videm V,Arnaout MAdoi
10.1016/0092-8674(93)90575-bsubject
Has Abstractpub_date
1993-03-26 00:00:00pages
857-67issue
6eissn
0092-8674issn
1097-4172pii
0092-8674(93)90575-Bjournal_volume
72pub_type
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