2JLP

Crystal structure of human extracellular copper-zinc superoxide dismutase.

2JLP の概要

• エントリーDOI: 10.2210/pdb2jlp/pdb
• 分子名称: EXTRACELLULAR SUPEROXIDE DISMUTASE (CU-ZN), COPPER (II) ION, ZINC ION, ... (5 entities in total)
• 機能のキーワード: glycolisation, oxidoreductase, heparin binding, heparin-binding, oxidative stress, antioxidant, glycoprotein, metal-binding, cu-zn, secreted, glycation
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 97419.34

構造登録者

Antonyuk, S.V.,Strange, R.W.,Marklund, S.L.,Hasnain, S.S. (登録日: 2008-09-14, 公開日: 2009-03-17, 最終更新日: 2024-11-20)

主引用文献

Antonyuk, S.V.,Strange, R.W.,Marklund, S.L.,Hasnain, S.S.
The Structure of Human Extracellular Copper-Zinc Superoxide Dismutase at 1.7 A Resolution: Insights Into Heparin and Collagen Binding.
J.Mol.Biol., 388:310-, 2009

PubMed Abstract: Extracellular superoxide dismutase (SOD3) is a homotetrameric copper- and zinc-containing glycoprotein with affinity for heparin. The level of SOD3 is particularly high in blood vessel walls and in the lungs. The enzyme has multiple roles including protection of the lungs against hyperoxia and preservation of nitric oxide. The common mutation R213G, which reduces the heparin affinity of SOD3, is associated with increased risk of myocardial infarctions and stroke. We report the first crystal structure of human SOD3 at 1.7 A resolution. The overall subunit fold and the subunit-subunit interface of the SOD3 dimer are similar to the corresponding structures in Cu-Zn SOD (SOD1). The metal-binding sites are similar to those found in SOD1, but with Asn180 replacing Thr137 at the Cu-binding site and a much shorter loop at the zinc-binding site. The dimers form a functional homotetramer that is fashioned through contacts between two extended loops on each subunit. The N- and C-terminal end regions required for tetramerisation and heparin binding, respectively, are highly flexible. Two grooves fashioned by the tetramer interface are suggestive as the probable sites for heparin and collagen binding.

PubMed: 19289127
DOI: 10.1016/J.JMB.2009.03.026

実験手法

X-RAY DIFFRACTION (1.7 Å)