1IJQ

Crystal Structure of the LDL Receptor YWTD-EGF Domain Pair

1IJQ の概要

• エントリーDOI: 10.2210/pdb1ijq/pdb
• 分子名称: LOW-DENSITY LIPOPROTEIN RECEPTOR (2 entities in total)
• 機能のキーワード: beta-propeller, lipid transport
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: 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: 71186.80

構造登録者

Jeon, H.,Meng, W.,Takagi, J.,Eck, M.J.,Springer, T.A.,Blacklow, S.C. (登録日: 2001-04-27, 公開日: 2001-05-23, 最終更新日: 2024-10-16)

主引用文献

Jeon, H.,Meng, W.,Takagi, J.,Eck, M.J.,Springer, T.A.,Blacklow, S.C.
Implications for familial hypercholesterolemia from the structure of the LDL receptor YWTD-EGF domain pair.
Nat.Struct.Biol., 8:499-504, 2001

PubMed Abstract: The low-density lipoprotein receptor (LDLR) is the primary mechanism for uptake of cholesterol-carrying particles into cells. The region of the LDLR implicated in receptor recycling and lipoprotein release at low pH contains a pair of calcium-binding EGF-like modules, followed by a series of six YWTD repeats and a third EGF-like module. The crystal structure at 1.5 A resolution of a receptor fragment spanning the YWTD repeats and its two flanking EGF modules reveals that the YWTD repeats form a six-bladed beta-propeller that packs tightly against the C-terminal EGF module, whereas the EGF module that precedes the propeller is disordered in the crystal. Numerous point mutations of the LDLR that result in the genetic disease familial hypercholesterolemia (FH) alter side chains that form conserved packing and hydrogen bonding interactions in the interior and between propeller blades. A second subset of FH mutations are located at the interface between the propeller and the C-terminal EGF module, suggesting a structural requirement for maintaining the integrity of the interdomain interface.

PubMed: 11373616
DOI: 10.1038/88556

実験手法

X-RAY DIFFRACTION (1.5 Å)