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2CWM

Native Crystal Structure of NO releasing inductive lectin from seeds of the Canavalia maritima (ConM)

2CWM の概要
エントリーDOI10.2210/pdb2cwm/pdb
分子名称lectin, CALCIUM ION, MANGANESE (II) ION, ... (4 entities in total)
機能のキーワードlectin, canavalia maritima, metal binding protein
由来する生物種Canavalia maritima
タンパク質・核酸の鎖数2
化学式量合計51178.42
構造登録者
主引用文献Gadelha, C.A.A.,Moreno, F.B.M.B.,Santi-Gadelha, T.,Cajazeiras, J.B.,Rocha, B.A.M.,Assreuy, A.M.S.,Lima Mota, M.R.,Pinto, N.V.,Passos Meireles, A.V.,Borges, J.C.,Freitas, B.T.,Canduri, F.,Souza, E.P.,Delatorre, P.,Criddle, D.N.,De Azevedo Jr., W.F.,Cavada, B.S.
Native crystal structure of a nitric oxide-releasing lectin from the seeds of Canavalia maritima
J.Struct.Biol., 152:185-194, 2005
Cited by
PubMed Abstract: Here, we report the crystallographic study of a lectin from Canavalia maritima seeds (ConM) and its relaxant activity on vascular smooth muscle, to provide new insights into the understanding of structure/function relationships of this class of proteins. ConM was crystallized and its structure determined by standard molecular replacement techniques. The amino acid residues, previously suggested incorrectly by manual sequencing, have now been determined as I17, I53, S129, S134, G144, S164, P165, S187, V190, S169, T196, and S202. Analysis of the structure indicated a dimer in the asymmetric unit, two metal binding sites per monomer, and loops involved in the molecular oligomerization. These confer 98% similarity between ConM and other previously described lectins, derived from Canavalia ensiformis and Canavalia brasiliensis. Our functional data indicate that ConM exerts a concentration-dependent relaxant action on isolated aortic rings that probably occurs via an interaction with a specific lectin-binding site on the endothelium, resulting in a release of nitric oxide.
PubMed: 16337811
DOI: 10.1016/j.jsb.2005.07.012
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.95 Å)
構造検証レポート
Validation report summary of 2cwm
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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