| LIM domain | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 Structure of the 4th LIM domain of Pinch protein. Zinc atoms are shown in grey | |||||||||||
| Identifiers | |||||||||||
| Symbol | LIM | ||||||||||
| Pfam | PF00412 | ||||||||||
| InterPro | IPR001781 | ||||||||||
| PROSITE | PDOC50178 | ||||||||||
| SCOP2 | 1ctl / SCOPe / SUPFAM | ||||||||||
| CDD | cd08368 | ||||||||||
| |||||||||||
LIM domains are protein structural domains, composed of two contiguous zinc fingers, separated by a two-amino acid residue hydrophobic linker.[1] The domain name is an acronym of the three genes in which it was first identified (LIN-11, Isl-1 and MEC-3).[2] LIM is a protein interaction domain that is involved in binding to many structurally and functionally diverse partners.[1] The LIM domain appeared in eukaryotes sometime prior to the most recent common ancestor of plants, fungi, amoeba and animals.[3] In animal cells, LIM domain-containing proteins often shuttle between the cell nucleus where they can regulate gene expression, and the cytoplasm where they are usually associated with actin cytoskeletal structures involved in connecting cells together and to the surrounding matrix, such as stress fibers, focal adhesions and adherens junctions.[1]
- ^ a b c Kadrmas JL, Beckerle MC (November 2004). "The LIM domain: from the cytoskeleton to the nucleus". Nature Reviews. Molecular Cell Biology. 5 (11): 920–31. doi:10.1038/nrm1499. PMID 15520811. S2CID 6030950.
- ^ Gill GN (December 1995). "The enigma of LIM domains". Structure. 3 (12): 1285–9. doi:10.1016/S0969-2126(01)00265-9. PMID 8747454.
- ^ Koch BJ, Ryan JF, Baxevanis AD (March 2012). "The diversification of the LIM superclass at the base of the metazoa increased subcellular complexity and promoted multicellular specialization". PLOS ONE. 7 (3): e33261. Bibcode:2012PLoSO...733261K. doi:10.1371/journal.pone.0033261. PMC 3305314. PMID 22438907.