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LIM domain
From Wikipedia, the free encyclopedia
'LIM domains' are protein structural domains, comprised of two contiguous zinc finger domains, separated by a two-amino acid residue hydrophobic linker. They are named after their initial discovery in the proteins Lin11, Isl-1 & Mec-3 [1]. LIM-domain containing proteins have been shown to play roles in cytoskeletal organisation, organ development and oncogenesis. LIM-domains mediate protein:protein interactions that are critical to cellular processes.
LIM domains have highly divergent sequences, apart from certain key residues. The sequence divergence allow a great many different binding sites to be grafted onto the same basic domain. The conserved residues are those involved in zinc binding or the hydrophobic core of the protein. The sequence signature of LIM domains are as follows:
[C]-[X]2-4-[C]-[X]13-19-[W]-[H]-[X]2-4-[C]-[F]-[LVI]-[C]-[X]2-4-[C]-[X]13-20-C-[X]2-4-[C]
LIM domains frequently occur in multiples, as seen in proteins such as TES, LMO4, and can also be attached to other domains in order to confer a binding or targeting function upon them, such as LIM-kinase.
- ^ Bach, I. The LIM domain: regulation by association (2000), Mech Devel, 91, p5-17
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BZIP - DED - Kringle - PH - SH2 - SH3 - zinc finger - coiled coil - helix bundle - globin fold - twisted open sheet - alpha/beta barrels - up and down barrel - greek key barrel - jelly roll barrel - greek key - leucine-rich repeat - beta propeller - LIM domain - C2 domain