Characterization of calcium and magnesium binding domains of human 5-lipoxygenase

Bindu, P. Hima ; Sastry, G. Madhavi ; Sastry, G. Narahari (2004) Characterization of calcium and magnesium binding domains of human 5-lipoxygenase Biochemical and Biophysical Research Communications, 320 (2). pp. 461-467. ISSN 0006-291X

Full text not available from this repository.

Official URL: http://www.sciencedirect.com/science/article/pii/S...

Related URL: http://dx.doi.org/10.1016/j.bbrc.2004.05.194

Abstract

Two calcium binding sites, separated by about 9.3 Å, present in the loops that connect the β-sheets of N-terminal domain contain the ligating residues F14, A15, G16, D79, and D18, D19, L76, respectively. Magnesium is found to bind in regions, which are marginally different owing to the disparity in the ionic radii of Ca2+ and Mg2+. The entropy analysis on the loops of 5-lipoxygenase, implementing the wormlike chain model, explains that the N-terminal β-barrel is well suited to accommodate calcium binding sites. The large buried side chain area of W102 (compared to W13 and W75) and comparatively smaller fraction of side chain exposed to polar atoms corroborate the calcium induced higher affinity to phosphatidylcholine (PC). However, W80 lying in close proximity of the calcium binding sites is expected to have considerable PC affinity but negligible calcium induced effect on PC binding.

Item Type:Article
Source:Copyright of this article belongs to Elsevier Science.
Keywords:5-Lipoxygenase; Calcium Binding Sites; Entropy Change; Tryptophan Residues; Homology Modeling
ID Code:106979
Deposited On:28 Jul 2017 09:26
Last Modified:28 Jul 2017 09:26

Repository Staff Only: item control page