1lox: Difference between revisions

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, ... [[http://ispc.weizmann.ac.il/pmbin/getpm?9406550 (full description)]]

1LOX is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus]] with FE2 and RS7 as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Arachidonate_15-lipoxygenase Arachidonate 15-lipoxygenase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.13.11.33 1.13.11.33]]. Structure known Active Site: NUL. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LOX OCA]].  

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