LisH domain

{{Infobox protein family

| Symbol = LisH

| Name = LisH

| image = PDB 1uuj EBI.jpg

| width =

| caption = n-terminal domain of lissencephaly-1 protein (lis-1)

| Pfam = PF08513

| Pfam_clan =

| InterPro = IPR013720

| SMART =

| PROSITE =

| MEROPS =

| SCOP =

| TCDB =

| OPM family =

| OPM protein =

| CAZy =

| CDD =

}}

In molecular biology, the LisH domain (lis homology domain) is a protein domain found in a large number of eukaryotic proteins, from metazoa, fungi and plants that have a wide range of functions. The recently solved structure of the LisH domain in the N-terminal region of LIS1 depicted it as a novel dimerisation motif, and that other structural elements are likely to play an important role in dimerisation.{{cite journal |vauthors=Kim MH, Cooper DR, Oleksy A, Devedjiev Y, Derewenda U, Reiner O, Otlewski J, Derewenda ZS | title = The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications | journal = Structure | volume = 12 | issue = 6 | pages = 987–98 |date=June 2004 | pmid = 15274919 | doi = 10.1016/j.str.2004.03.024 | doi-access = free }}{{cite journal |vauthors=Mateja A, Cierpicki T, Paduch M, Derewenda ZS, Otlewski J | title = The dimerization mechanism of LIS1 and its implication for proteins containing the LisH motif | journal = J. Mol. Biol. | volume = 357 | issue = 2 | pages = 621–31 |date=March 2006 | pmid = 16445939 | doi = 10.1016/j.jmb.2006.01.002 }}{{cite journal |vauthors=Gerlitz G, Darhin E, Giorgio G, Franco B, Reiner O | title = Novel functional features of the Lis-H domain: role in protein dimerization, half-life and cellular localization | journal = Cell Cycle | volume = 4 | issue = 11 | pages = 1632–40 |date=November 2005 | pmid = 16258276 | doi = 10.4161/cc.4.11.2151| doi-access = free }}

The LisH domain is found in the Saccharomyces cerevisiae SIF2 protein, a component of the SET3 complex which is responsible for repressing meiotic genes In SIF2 the LisH domain has been shown to mediate dimer and tetramer formation.{{cite journal|vauthors=Cerna D, Wilson DK | title=The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex. | journal=J Mol Biol | year= 2005 | volume= 351 | issue= 4 | pages= 923–35 | pmid=16051270 | doi=10.1016/j.jmb.2005.06.025 }} It has been shown that the LisH domain helps mediate interaction with components of the SET3 complex.