Structural features of the low-density lipoprotein receptor facilitating ligand binding and release

Authors
Beglova, NJeon, HFisher, CBlacklow, SC
Issue Date
2004-11
Publisher
PORTLAND PRESS LTD
Citation
BIOCHEMICAL SOCIETY TRANSACTIONS, v.32, pp.721 - 723
Abstract
The LDLR (low-density lipoprotein receptor) is a modular protein built from several distinct structural units: LA (LDLR type-A), epidermal growth factor-like and beta-propeller modules. The low pH X-ray structure of the LDLR revealed long-range intramolecular contacts between the propeller domain and the central LA repeats of the ligand-binding domain, suggesting that the receptor changes its overall shape from extended to closed, in response to pH. Here we discuss how the LDLR uses flexibility and rigidity of linkers between modules to facilitate ligand binding and low-pH ligand release.
Keywords
HUMAN APOLIPOPROTEIN-E; LDL RECEPTOR; FAMILIAL HYPERCHOLESTEROLEMIA; BACKBONE DYNAMICS; NMR STRUCTURE; DOMAIN; PAIR; CONCATEMER; MODULES; HUMAN APOLIPOPROTEIN-E; LDL RECEPTOR; FAMILIAL HYPERCHOLESTEROLEMIA; BACKBONE DYNAMICS; NMR STRUCTURE; DOMAIN; PAIR; CONCATEMER; MODULES; conformational change; interdomain linkers; ligand binding; lipoprotein; NMR; structure
ISSN
0300-5127
URI
https://pubs.kist.re.kr/handle/201004/137121
DOI
10.1042/BST0320721
Appears in Collections:
KIST Article > 2004
Files in This Item:
There are no files associated with this item.
Export
RIS (EndNote)
XLS (Excel)
XML

qrcode

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.

BROWSE