1997
DOI: 10.1091/mbc.8.2.219
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Molecular dissection of a LIM domain.

Abstract: LIM domains are novel sequence elements that are found in more than 60 gene products, many of which function as key regulators of developmental pathways. The LIM domain, characterized by the cysteine-rich consensus CX2CX16-23HX2CX2CX2CX16-21 CX2-3(C/H/ D), is a specific mental-binding structure that consists of two distinct zinc-binding subdomains. We and others have recently demonstrated that the LIM domain mediates protein-protein interactions. However, the sequences that define the protein-binding specifici… Show more

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Cited by 93 publications
(100 citation statements)
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“…They are thought to function as versatile protein modules, capable of acting within diverse cellular contexts and in multiple subcellular compartments. Many have been shown to participate in direct protein-protein interactions, and they may also have the capacity to bind DNA directly (5,17,34). Structural analysis of LIM domains suggest that most adopt a similar zinc-bound finger; however, no protein has been identified as a common target for LIM domains (28).…”
mentioning
confidence: 99%
“…They are thought to function as versatile protein modules, capable of acting within diverse cellular contexts and in multiple subcellular compartments. Many have been shown to participate in direct protein-protein interactions, and they may also have the capacity to bind DNA directly (5,17,34). Structural analysis of LIM domains suggest that most adopt a similar zinc-bound finger; however, no protein has been identified as a common target for LIM domains (28).…”
mentioning
confidence: 99%
“…The animal LIMs are one of the widely studied LIM proteins known in eukaryotes and provide function related to development and disease (Hobert and Westphal 2000;Kadrmas and Beckerle 2004;Matthews et al 2013). The known LIM domain in the plant always has either H (in 2LIMs) or C (in DA1/DAR) as last amino acid residue and not D (aspartate) which is reported in some animal CRPs (Schmeichel and Beckerle 1997). Moreover, the plant LIM proteins also have comparatively longer C-terminal and are short of glycine-rich region (GRR) following each LIM domain (Arnaud et al 2007).…”
Section: Architecture Of Lim Domainmentioning
confidence: 99%
“…The individual LIM domain was recognized as a protein-protein interaction module which represents a consensus sequence as [C-X 2 -C-X 16-23 -H-X 2 -C]-X 2 -[C-X 2 -C-X 16-21 C-X 2-3 -(C/D/H)] (Kadrmas and Beckerle 2004). The universal make-up of LIM domain comprises two zinc fingers linked together with a short two-amino acid spacer (Sadler et al 1992;Pérez-Alvarado et al 1994;Schmeichel and Beckerle 1997;Yao et al 1999). This protein family has been addressed for features related to animal system mostly covering the aspects of cytoskeletal organization, development and diseases (Zheng and Zhao 2007).…”
Section: Introductionmentioning
confidence: 99%
“…The LIM domain is a tandem zinc finger motif of (55 amino acids that basically function in protein-protein interactions) [Schmeichel and Beckerle, 1997;Kadrmas and Beckerle, 2004]. Whereas animals possess numerous LIM proteins of diverse structures and functions, plants only contain a limited number of LIM proteins [Arnaud et al, 2007].…”
Section: Lim Proteinsmentioning
confidence: 99%