1AJJ

LDL RECEPTOR LIGAND-BINDING MODULE 5, CALCIUM-COORDINATING

Summary for 1AJJ

• Entry DOI: 10.2210/pdb1ajj/pdb
• Descriptor: LOW-DENSITY LIPOPROTEIN RECEPTOR, SULFATE ION, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: receptor, ldl receptor, cysteine-rich module, calcium
• Biological source: Homo sapiens (human)
• Cellular location: Cell membrane; Single-pass type I membrane protein: P01130
• Total number of polymer chains: 1
• Total formula weight: 4205.57

Authors

Fass, D.,Blacklow, S.C.,Kim, P.S.,Berger, J.M. (deposition date: 1997-05-04, release date: 1997-07-07, Last modification date: 2011-07-13)

Primary citation

Fass, D.,Blacklow, S.,Kim, P.S.,Berger, J.M.
Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module.
Nature, 388:691-693, 1997

PubMed Abstract: The low-density lipoprotein receptor (LDLR) is responsible for the uptake of cholesterol-containing lipoprotein particles into cells. The amino-terminal region of LDLR, which consists of seven tandemly repeated, approximately 40-amino-acid, cysteine-rich modules (LDL-A modules), mediates binding to lipoproteins. LDL-A modules are biologically ubiquitous domains, found in over 100 proteins in the sequence database. The structure of ligand-binding repeat 5 (LR5) of the LDLR, determined to 1.7 A resolution by X-ray crystallography and presented here, contains a calcium ion coordinated by acidic residues that lie at the carboxy-terminal end of the domain and are conserved among LDL-A modules. Naturally occurring point mutations found in patients with the disease familial hypercholesterolaemia alter residues that directly coordinate Ca2+ or that serve as scaffolding residues of LR5.

PubMed: 9262405
DOI: 10.1038/41798

Experimental method

X-RAY DIFFRACTION (1.7 Å)