2LGP

Solution structure of LA45 from LDLR

2LGP の概要

• エントリーDOI: 10.2210/pdb2lgp/pdb
• NMR情報: BMRB: 16480
• 分子名称: Low-density lipoprotein receptor, CALCIUM ION (2 entities in total)
• 機能のキーワード: complement repeat, protein binding
• 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: 1
• 化学式量合計: 10249.19

構造登録者

Guttman, M.,Komives, E.A. (登録日: 2011-08-01, 公開日: 2011-11-30, 最終更新日: 2024-10-30)

主引用文献

Guttman, M.,Komives, E.A.
The Structure, Dynamics, and Binding of the LA45 Module Pair of the Low-Density Lipoprotein Receptor Suggest an Important Role for LA4 in Ligand Release.
Biochemistry, 50:11001-11008, 2011

PubMed Abstract: The low-density lipoprotein receptor (LDLR), the primary receptor for cholesterol uptake, binds ligands through its seven LDL-A modules (LAs). We present nuclear magnetic resonance (NMR) and ligand binding measurements on the fourth and fifth modules of the LDLR (LA45), the modules critical for ApoE binding, at physiological pH. Unlike LA5 and all other modules in LDLR, LA4 has a very weak calcium affinity, which probably plays a critical role in endosomal ligand release. The NMR solution structure of each module in the LA45 pair only showed minor differences compared to the analogous domains in previously determined crystal structures. The 12-residue linker connecting the modules, though slightly structured through an interaction with LA4, is highly flexible. Although no intermodule nuclear Overhauser effects were detected, chemical shift perturbations and backbone dynamics suggest cross talk between the two modules. The ligand affinity of both modules is enhanced when the two are linked. LA4 is more flexible than LA5 and remains so even in the module pair, which likely is related to its weaker calcium binding affinity.

PubMed: 22091758
DOI: 10.1021/bi2014486

実験手法

SOLUTION NMR