1AJJ
LDL RECEPTOR LIGAND-BINDING MODULE 5, CALCIUM-COORDINATING
1AJJ の概要
エントリーDOI | 10.2210/pdb1ajj/pdb |
分子名称 | LOW-DENSITY LIPOPROTEIN RECEPTOR, SULFATE ION, CALCIUM ION, ... (4 entities in total) |
機能のキーワード | receptor, ldl receptor, cysteine-rich module, calcium |
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 | 4205.57 |
構造登録者 | Fass, D.,Blacklow, S.C.,Kim, P.S.,Berger, J.M. (登録日: 1997-05-04, 公開日: 1997-07-07, 最終更新日: 2011-07-13) |
主引用文献 | Fass, D.,Blacklow, S.,Kim, P.S.,Berger, J.M. Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module. Nature, 388:691-693, 1997 Cited by PubMed Abstract: The low-density lipoprotein receptor (LDLR) is responsible for the uptake of cholesterol-containing lipoprotein particles into cells. The amino-terminal region of LDLR, which consists of seven tandemly repeated, approximately 40-amino-acid, cysteine-rich modules (LDL-A modules), mediates binding to lipoproteins. LDL-A modules are biologically ubiquitous domains, found in over 100 proteins in the sequence database. The structure of ligand-binding repeat 5 (LR5) of the LDLR, determined to 1.7 A resolution by X-ray crystallography and presented here, contains a calcium ion coordinated by acidic residues that lie at the carboxy-terminal end of the domain and are conserved among LDL-A modules. Naturally occurring point mutations found in patients with the disease familial hypercholesterolaemia alter residues that directly coordinate Ca2+ or that serve as scaffolding residues of LR5. PubMed: 9262405DOI: 10.1038/41798 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.7 Å) |
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