Biology:LisH domain
| LisH | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 n-terminal domain of lissencephaly-1 protein (lis-1) | |||||||||
| Identifiers | |||||||||
| Symbol | LisH | ||||||||
| Pfam | PF08513 | ||||||||
| InterPro | IPR013720 | ||||||||
| |||||||||
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.[1][2][3]
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.[4] It has been shown that the LisH domain helps mediate interaction with components of the SET3 complex.[4]
References
- ↑ "The structure of the N-terminal domain of the product of the lissencephaly gene Lis1 and its functional implications". Structure 12 (6): 987–98. June 2004. doi:10.1016/j.str.2004.03.024. PMID 15274919.
- ↑ "The dimerization mechanism of LIS1 and its implication for proteins containing the LisH motif". J. Mol. Biol. 357 (2): 621–31. March 2006. doi:10.1016/j.jmb.2006.01.002. PMID 16445939.
- ↑ "Novel functional features of the Lis-H domain: role in protein dimerization, half-life and cellular localization". Cell Cycle 4 (11): 1632–40. November 2005. doi:10.4161/cc.4.11.2151. PMID 16258276.
- ↑ 4.0 4.1 "The structure of Sif2p, a WD repeat protein functioning in the SET3 corepressor complex.". J Mol Biol 351 (4): 923–35. 2005. doi:10.1016/j.jmb.2005.06.025. PMID 16051270.
 |  |
