4OY9
Crystal structure of human P-Cadherin EC1-EC2 in closed conformation
4OY9 の概要
エントリーDOI | 10.2210/pdb4oy9/pdb |
分子名称 | Cadherin-3, CALCIUM ION (3 entities in total) |
機能のキーワード | adhesion, cadherin, calcium-binding protein., cell adhesion |
由来する生物種 | Homo sapiens (Human) |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 23411.05 |
構造登録者 | Dalle Vedove, A.,Lucarelli, A.P.,Nardone, V.,Matino, A.,Parisini, E. (登録日: 2014-02-11, 公開日: 2015-04-01, 最終更新日: 2023-12-27) |
主引用文献 | Dalle Vedove, A.,Lucarelli, A.P.,Nardone, V.,Matino, A.,Parisini, E. The X-ray structure of human P-cadherin EC1-EC2 in a closed conformation provides insight into the type I cadherin dimerization pathway. Acta Crystallogr.,Sect.F, 71:371-380, 2015 Cited by PubMed Abstract: Cadherins are a large family of calcium-dependent proteins that mediate cellular adherens junction formation and tissue morphogenesis. To date, the most studied cadherins are those classified as classical, which are further divided into type I or type II depending on selected sequence features. Unlike other members of the classical cadherin family, a detailed structural characterization of P-cadherin has not yet been fully obtained. Here, the high-resolution crystal structure determination of the closed form of human P-cadherin EC1-EC2 is reported. The structure shows a novel, monomeric packing arrangement that provides a further snapshot in the yet-to-be-achieved complete description of the highly dynamic cadherin dimerization pathway. Moreover, this is the first multidomain cadherin fragment to be crystallized and structurally characterized in its closed conformation that does not carry any extra N-terminal residues before the naturally occurring aspartic acid at position 1. Finally, two clear alternate conformations are observed for the critical Trp2 residue, suggestive of a transient, metastable state. The P-cadherin structure and packing arrangement shown here provide new and valuable information towards the complete structural characterization of the still largely elusive cadherin dimerization pathway. PubMed: 25849494DOI: 10.1107/S2053230X15003878 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.62 Å) |
構造検証レポート
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