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ABSTRACT: Background
The binding of ligands to clusters of complement-type repeat (CR)-domains in proteins of the low-density lipoprotein receptor (LDLR) family is dependent on Ca2+ ions. One reason for this cation requirement was identified from the crystal structure data for a CR-domain from the prototypic LDLR, which showed the burial of a Ca2+ ion as a necessity for correct folding and stabilization of this protein module. Additional Ca2+ binding data to other CR-domains from both LDLR and the LDLR-related protein (LRP) have suggested the presence of a conserved Ca2+ cage within CR-domains from this family of receptors that function in endocytosis and signalling.Results
We have previously described the binding of several ligands to a fragment comprising the fifth and the sixth CR
SUBMITTER: Andersen OM
PROVIDER: S-EPMC194729 | biostudies-literature | 2003 Aug
REPOSITORIES: biostudies-literature