3FE4

Crystal Structure of Human Carbonic Anhydrase vi

3FE4 の概要

• エントリーDOI: 10.2210/pdb3fe4/pdb
• 分子名称: Carbonic anhydrase 6, MAGNESIUM ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: carbonic anhydrase, secretion, metal binding, structural genomics, structural genomics consortium, sgc, glycoprotein, lyase, metal-binding, secreted
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Secreted: P23280
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 64133.81

構造登録者

Pilka, E.S.,Kochan, G.,Krysztofinska, E.,Muniz, J.,Yue, W.W.,Roos, A.K.,von Delft, F.,Arrowsmith, C.H.,Weigelt, J.,Edwards, A.,Bountra, C.,Oppermann, U.,Structural Genomics Consortium (SGC) (登録日: 2008-11-27, 公開日: 2008-12-16, 最終更新日: 2024-10-09)

主引用文献

Pilka, E.S.,Kochan, G.,Oppermann, U.,Yue, W.W.
Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development
Biochem.Biophys.Res.Commun., 419:485-489, 2012

PubMed Abstract: Zn(2+)-dependent carbonic anhydrases (CA) catalyse the reversible hydration of carbon dioxide to bicarbonate and participate in diverse physiological processes, hence having manifold therapeutic potentials. Among the 15 human CAs with wide-ranging sub-cellular localisation and kinetic properties, CA VI is the only secretory isoform. The 1.9Å crystal structure of the human CA VI catalytic domain reveals a prototypical mammalian CA fold, and a novel dimeric arrangement as compared to previously-reported CA structures. The active site cavity contains a cluster of non-conserved residues that may be involved in ligand binding and have significant implications for developing the next-generation of isoform-specific inhibitors.

PubMed: 22366092
DOI: 10.1016/j.bbrc.2012.02.038

実験手法

X-RAY DIFFRACTION (1.9 Å)