LisHLissencephaly type-1-like homology motif
|SMART accession number:||SM00667|
|Description:||Alpha-helical motif present in Lis1, treacle, Nopp140, some katanin p60 subunits, muskelin, tonneau, LEUNIG and numerous WD40 repeat-containing proteins. It is suggested that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly.|
|Interpro abstract (IPR006594):|
The 33-residue LIS1 homology (LisH) motif is found in eukaryotic intracellular proteins involved in microtubule dynamics, cell migration, nucleokinesis and chromosome segregation. The LisH motif is likely to possess a conserved protein-binding function and it has been proposed that LisH motifs contribute to the regulation of microtubule dynamics, either by mediating dimerisation, or else by binding cytoplasmic dynein heavy chain or microtubules directly. The LisH motif is found associated to other domains, such as WD-40, SPRY, Kelch, AAA ATPase, RasGEF, or HEAT [(PUBMED:11734546), (PUBMED:12384287), (PUBMED:12559565)].
The secondary structure of the LisH domain is predicted to be two alpha- helices [(PUBMED:11734546)].
|GO function:||protein binding (GO:0005515)|
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