In molecular biology, theLisH domain (lis homology domain) is aprotein domain found in a large number ofeukaryoticproteins, frommetazoa,fungi andplants that have a wide range of functions. The recently solvedstructure of the LisH domain in theN-terminal region ofLIS1 depicted it as a noveldimerisation motif, and that other structural elements are likely to play an important role in dimerisation.[1][2][3]
The LisH domain is found in theSaccharomyces cerevisiae SIF2 protein, a component of the SET3complex which is responsible for repressingmeioticgenes In SIF2 the LisH domain has been shown to mediate dimer and tetramer formation.[4] It has been shown that the LisH domain helps mediate interaction with components of the SET3 complex.[4]
^Mateja A, Cierpicki T, Paduch M, Derewenda ZS, Otlewski J (March 2006). "The dimerization mechanism of LIS1 and its implication for proteins containing the LisH motif".J. Mol. Biol.357 (2):621–31.doi:10.1016/j.jmb.2006.01.002.PMID16445939.
^abCerna D, Wilson DK (2005). "The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex".J Mol Biol.351 (4):923–35.doi:10.1016/j.jmb.2005.06.025.PMID16051270.
