3P5C

The structure of the LDLR/PCSK9 complex reveals the receptor in an extended conformation

3P5C の概要

• エントリーDOI: 10.2210/pdb3p5c/pdb
• 関連するPDBエントリー: 3P5B
• 分子名称: Proprotein convertase subtilisin/kexin type 9, Low density lipoprotein receptor variant, CALCIUM ION, ... (4 entities in total)
• 機能のキーワード: b-propellor, receptor, convertase, hydrolase-lipid binding protein complex, hydrolase/lipid binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Cytoplasm: Q8NBP7 Q8NBP7
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 117293.73

構造登録者

Lo Surdo, P.,Bottomley, M.J.,Calzetta, A.,Settembre, E.C.,Cirillo, A.,Pandit, S.,Ni, Y.,Hubbard, B.,Sitlani, A.,Carfi, A. (登録日: 2010-10-08, 公開日: 2011-10-26, 最終更新日: 2024-11-06)

主引用文献

Lo Surdo, P.,Bottomley, M.J.,Calzetta, A.,Settembre, E.C.,Cirillo, A.,Pandit, S.,Ni, Y.G.,Hubbard, B.,Sitlani, A.,Carfi, A.
Mechanistic implications for LDL receptor degradation from the PCSK9/LDLR structure at neutral pH.
Embo Rep., 12:1300-1305, 2011

PubMed Abstract: The protein PCSK9 (proprotein convertase subtilisin/kexin type 9) is a key regulator of low-density lipoprotein receptor (LDLR) levels and cardiovascular health. We have determined the crystal structure of LDLR bound to PCSK9 at neutral pH. The structure shows LDLR in a new extended conformation. The PCSK9 C-terminal domain is solvent exposed, enabling cofactor binding, whereas the catalytic domain and prodomain interact with LDLR epidermal growth factor(A) and β-propeller domains, respectively. Thus, PCSK9 seems to hold LDLR in an extended conformation and to interfere with conformational rearrangements required for LDLR recycling.

PubMed: 22081141
DOI: 10.1038/embor.2011.205

実験手法

X-RAY DIFFRACTION (4.2 Å)