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Nat Struct Biol. 1997 Dec;4(12):1003-9.

The structure of mammalian 15-lipoxygenase reveals similarity to the lipases and the determinants of substrate specificity.

Author information

1
Graduate Group in Biophysics, University of California, San Francisco 94143-0448, USA.

Erratum in

  • Nat Struct Biol 1998 Mar;5(3):242.

Abstract

Here we report the first structure of a mammalian 15-lipoxygenase. The protein is composed of two domains; a catalytic domain and a previously unrecognized beta-barrel domain. The N-terminal beta-barrel domain has topological and sequence identify to a domain in the mammalian lipases, suggesting that these domains may have similar functions in vivo. Within the C-terminal domain, the lipoxygenase substrate binding site is a hydrophobic pocket defined by a bound inhibitor. Arachidonic acid can be docked into this deep hydrophobic pocket with the methyl end extending down into the bottom of the pocket and the acid end tethered by a conserved basic residue on the surface of the enzyme. This structure provides a unifying hypothesis for the positional specificity of mammalian lipoxygenases.

PMID:
9406550
[Indexed for MEDLINE]

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