2003
DOI: 10.1021/bi0269714
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C-Terminal Half of Human Centrin 2 Behaves like a Regulatory EF-Hand Domain

Abstract: Human centrin 2 (HsCen2) is an EF-hand protein that plays a critical role in the centrosome duplication and separation during cell division. We studied the structural and Ca(2+)-binding properties of two C-terminal fragments of this protein: SC-HsCen2 (T94-Y172), covering two EF-hands, and LC-HsCen2 (M84-Y172), having 10 additional residues. Both fragments are highly disordered in the apo state but become better structured (although not conformationally homogeneous) in the presence of Ca(2+) and depending on t… Show more

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Cited by 69 publications
(151 citation statements)
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References 38 publications
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“…Full length human centrin-2 (HsCen-2), and the carboxyl-terminal domains of HsCen-2 fragments, bind calcium at one high affinity site, probably in the most carboxyl-terminal EF-hand [19,20]. Previous studies suggested that HsCen-2 is dimeric and binds only two calciums per dimer, likely to site IV in each monomer [19].…”
mentioning
confidence: 99%
“…Full length human centrin-2 (HsCen-2), and the carboxyl-terminal domains of HsCen-2 fragments, bind calcium at one high affinity site, probably in the most carboxyl-terminal EF-hand [19,20]. Previous studies suggested that HsCen-2 is dimeric and binds only two calciums per dimer, likely to site IV in each monomer [19].…”
mentioning
confidence: 99%
“…In agreement with this, only the C-terminal half of centrin 2 may be required for interaction with XPC (10,31,46). Although the primary amino acid sequence of the centrin 2-binding domain of XPC is classified as a 1-14 motif, the structural basis of complex formation may be different than that for typical calmodulin complexes like smMLCK and skMLCK.…”
mentioning
confidence: 76%
“…In the absence of both HR23 proteins, XPC is markedly destabilized in vivo as well as in vitro, and thus, the HR23 proteins are effectively essential for efficient GG-NER (2,5,40,43). A recombinant XPC-HR23B heterodimer exhibits specific binding affinities for various types of lesions, including 6-4PP, and has been successfully used to reconstitute a cell-free NER reaction (1,3,31). Centrin 2 is thus dispensable for NER at least in vitro, so the biological significance of its presence in the XPC complex remains to be elucidated, although the physical stability of XPC-HR23B may increase slightly upon binding to centrin 2 (2).…”
mentioning
confidence: 99%
“…The region is of interest, because it is not present in any other members of the calmodulin-parvalbumin superfamily. Titrating HsCen-2 (26,43) and other centrins (44) to Ca 2Ï© saturation is complicated by aggregation of high order oligomers, an aggregation of reversible nature. Deletion of amino acids 1-24 has little effect on protein stability, global secondary structure, or metal binding (29) but does prevent aggregation; thus, these residues must be involved in the self-assembly (45).…”
Section: Disordered Hscen-2 N-terminalmentioning
confidence: 99%