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spinqualitylabelsall models 2fcw, resolution 1.26Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Structure of a Complex Between the Pair of the LDL Receptor Ligand-Binding Modules 3-4 and the Receptor Associated Protein (RAP).

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Proteins of the low-density lipoprotein receptor (LDLR) family are remarkable in their ability to bind an extremely diverse range of protein and lipoprotein ligands, yet the basis for ligand recognition is poorly understood. Here, we report the 1.26 A X-ray structure of a complex between a two-module region of the ligand binding domain of the LDLR and the third domain of RAP, an escort protein for LDLR family members. The RAP domain forms a three-helix bundle with two docking sites, one for each LDLR module. The mode of recognition at each site is virtually identical: three conserved, calcium-coordinating acidic residues from each LDLR module encircle a lysine side chain protruding from the second helix of RAP. This metal-dependent mode of electrostatic recognition, together with avidity effects resulting from the use of multiple sites, represents a general binding strategy likely to apply in the binding of other basic ligands to LDLR family proteins.

Disease

Known disease associated with this structure: Hypercholesterolemia, familial OMIM:[606945]

About this Structure

2FCW is a Protein complex structure of sequences from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors., Fisher C, Beglova N, Blacklow SC, Mol Cell. 2006 Apr 21;22(2):277-83. PMID:16630895

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