2FCW

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

2FCW の概要

• エントリーDOI: 10.2210/pdb2fcw/pdb
• 分子名称: Alpha-2-macroglobulin receptor-associated protein, Low-density lipoprotein receptor, SODIUM ION, ... (6 entities in total)
• 機能のキーワード: protein-protein complex, rap, ldlr, escort protein, calcium-binding, lipid transport-endocytosis-chaperone complex, lipid transport/endocytosis/chaperone
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Endoplasmic reticulum: P30533; Cell membrane; Single-pass type I membrane protein: P01130
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 22363.92

構造登録者

Beglova, N.,Fisher, C.,Blacklow, S.C. (登録日: 2005-12-12, 公開日: 2006-05-16, 最終更新日: 2024-04-03)

主引用文献

Fisher, C.,Beglova, N.,Blacklow, S.C.
Structure of an LDLR-RAP Complex Reveals a General Mode for Ligand Recognition by Lipoprotein Receptors
Mol.Cell, 22:277-283, 2006

PubMed Abstract: 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.

PubMed: 16630895
DOI: 10.1016/j.molcel.2006.02.021

実験手法

X-RAY DIFFRACTION (1.26 Å)