1LDL

THREE-DIMENSIONAL STRUCTURE OF A CYSTEINE-RICH REPEAT FROM THE LOW-DENSITY LIPOPROTEIN RECEPTOR

1LDL の概要

• エントリーDOI: 10.2210/pdb1ldl/pdb
• 分子名称: LOW-DENSITY LIPOPROTEIN RECEPTOR (1 entity in total)
• 機能のキーワード: ldl receptor cysteine-rich repeat, binding protein
• 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: 5229.60

構造登録者

Daly, N.L.,Scanlon, M.J.,Kroon, P.A.,Smith, R. (登録日: 1995-03-20, 公開日: 1996-03-08, 最終更新日: 2024-10-30)

主引用文献

Daly, N.L.,Scanlon, M.J.,Djordjevic, J.T.,Kroon, P.A.,Smith, R.
Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor.
Proc.Natl.Acad.Sci.USA, 92:6334-6338, 1995

PubMed Abstract: The low-density lipoprotein (LDL) receptor plays a central role in mammalian cholesterol metabolism, clearing lipoproteins which bear apolipoproteins E and B-100 from plasma. Mutations in this molecule are associated with familial hypercholesterolemia, a condition which leads to an elevated plasma cholesterol concentration and accelerated atherosclerosis. The N-terminal segment of the LDL receptor contains a heptad of cysteine-rich repeats that bind the lipoproteins. Similar repeats are present in related receptors, including the very low-density lipoprotein receptor and the LDL receptor-related protein/alpha 2-macroglobulin receptor, and in proteins which are functionally unrelated, such as the C9 component of complement. The first repeat of the human LDL receptor has been expressed in Escherichia coli as a glutathione S-transferase fusion protein, and the cleaved and purified receptor module has been shown to fold to a single, fully oxidized form that is recognized by the monoclonal antibody IgG-C7 in the presence of calcium ions. The three-dimensional structure of this module has been determined by two-dimensional NMR spectroscopy and shown to consist of a beta-hairpin structure, followed by a series of beta turns. Many of the side chains of the acidic residues, including the highly conserved Ser-Asp-Glu triad, are clustered on one face of the module. To our knowledge, this structure has not previously been described in any other protein and may represent a structural paradigm both for the other modules in the LDL receptor and for the homologous domains of several other proteins. Calcium ions had only minor effects on the CD spectrum and no effect on the 1H NMR spectrum of the repeat, suggesting that they induce no significant conformational change.

PubMed: 7603991
DOI: 10.1073/pnas.92.14.6334

実験手法

SOLUTION NMR