LIM domain LIM domains are protein structural domains, composed 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 L in11, I sl-1 & M ec-3.
Zinc fingers, piccolo-type Piccolo zinc fingers were found to interact with the dual prenylated rab3A and VAMP2/Synaptobrevin II receptor PRA1. There are eight conserved cysteines in Piccolo-type zinc fingers, suggesting that they coordinate two zinc ligands. [Source: InterPro]
Zinc fingers, TRAF-type This gene group contains genes that encode proteins with a TRAF-type zinc finger domain. Some of the proteins that have this domain are mammalian signal transducers associated with the cytoplasmic domain of the 75kDa tumour necrosis factor receptor. A heterocomplex, homodimer or heterodimer of TRAF1 and TRAF2, binds to the N-terminal of the inhibitor of apoptosis proteins 1 and 2 (IAPS) and recruits them to the tumour necrosis factor receptor 2. [Source: InterPro]
