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Titre du document / Document title

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

Auteur(s) / Author(s)


Résumé / Abstract

Two calcium binding sites, separated by about 9.3 A, 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.

Revue / Journal Title

Biochemical and biophysical research communications    ISSN  0006-291X   CODEN BBRCA9 

Source / Source

2004, vol. 320, no2, pp. 461-467 [7 page(s) (article)]

Langue / Language


Editeur / Publisher

Elsevier, Amsterdam, PAYS-BAS  (1959) (Revue)

Localisation / Location

INIST-CNRS, Cote INIST : 8252, 35400011371375.0280

Nº notice refdoc (ud4) : 15940682

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