Lipoxygenase homology 2 (beta barrel) domain
SMART accession number:SM00308
Interpro abstract (IPR001024):

Lipoxygenases (EC 1.13.11.-) are a class of iron-containing dioxygenases which catalyses the hydroperoxidation of lipids, containing a cis,cis-1,4-pentadiene structure. They are common in plants where they may be involved in a number of diverse aspects of plant physiology including growth and development, pest resistance, and senescence or responses to wounding. In mammals a number of lipoxygenases isozymes are involved in the metabolism of prostaglandins and leukotrienes [(PUBMED:3017195)]. Sequence data is available for the following lipoxygenases:

The iron atom in lipoxygenases is bound by four ligands, three of which are histidine residues [(PUBMED:8502991)]. Six histidines are conserved in all lipoxygenase sequences, five of them are found clustered in a stretch of 40 amino acids. This region contains two of the three iron-ligands; the other histidines have been shown [(PUBMED:1567851)] to be important for the activity of lipoxygenases.

This entry represents a domain found in lipoxygenases and other enzymes. It is known as the PLAT (Polycystin-1, Lipoxygenase, Alpha-Toxin) domain or LH2 (Lipoxygenase homology) domain, is found in a variety of membrane or lipid associated proteins. Structurally, this domain forms a beta-sandwich composed of two sheets of four strands each [(PUBMED:10469604), (PUBMED:11985859), (PUBMED:11412104)]. The most highly conserved regions coincide with the beta-strands, with most of the highly conserved residues being buried within the protein. An exception to this is a surface lysine or arginine that occurs on the surface of the fifth beta-strand of the eukaryotic domains. In pancreatic lipase, the lysine in this position forms a salt bridge with the procolipase protein. The conservation of a charged surface residue may indicate the location of a conserved ligand-binding site. It is thought that this domain may mediate membrane attachment via other protein binding partners.

GO function:protein binding (GO:0005515)
Family alignment:
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There are 0 LH2 domains in 0 proteins in SMART's nrdb database.

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