Please use this identifier to cite or link to this item:
https://scholarbank.nus.edu.sg/handle/10635/111804
DC Field | Value | |
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dc.title | Breakpoint cluster region gene product-related domain of n-chimaerin: Discrimination between Rac-binding and GTPase-activating residues by mutational analysis | |
dc.contributor.author | Ahmed, S. | |
dc.contributor.author | Lee, J. | |
dc.contributor.author | Wen, L.-P. | |
dc.contributor.author | Zhao, Z. | |
dc.contributor.author | Ho, J. | |
dc.contributor.author | Best, A. | |
dc.contributor.author | Kozma, R. | |
dc.contributor.author | Lim, L. | |
dc.date.accessioned | 2014-11-28T02:49:52Z | |
dc.date.available | 2014-11-28T02:49:52Z | |
dc.date.issued | 1994-07-01 | |
dc.identifier.citation | Ahmed, S.,Lee, J.,Wen, L.-P.,Zhao, Z.,Ho, J.,Best, A.,Kozma, R.,Lim, L. (1994-07-01). Breakpoint cluster region gene product-related domain of n-chimaerin: Discrimination between Rac-binding and GTPase-activating residues by mutational analysis. Journal of Biological Chemistry 269 (26) : 17642-17648. ScholarBank@NUS Repository. | |
dc.identifier.issn | 00219258 | |
dc.identifier.uri | http://scholarbank.nus.edu.sg/handle/10635/111804 | |
dc.description.abstract | The breakpoint cluster region gene product (Bcr) is a GTPase-activating protein (GAP) for members of the Rho family, Cdc42Hs, and Racl, as is the brain protein n-chimaerin. At least 15 proteins have sequence identity to the GAP domain (150 amino acid residues) of Bcr. The widespread occurrence of proteins that possess sequence identity to the Bcr-related GAP domain makes it especially important to understand its structure/ function relationships. Amino acid sequence alignment of these proteins reveals three blocks of conservation in the GAP domain. Here, we present a mutational analysis of this domain using n-chimaerin sequences. Ten mutations were constructed (at least two in each of the blocks of conservation), expressed as glutathione S-transferase fusion proteins in Escherichia coli, and purified. Seven of the mutants, including deletions, still possessed GAP activity for Rac1. Three of the mutants had no Rac1-GAP activity but were still able to bind Rac1. IC50 values obtained from competition experiments suggest that ra-chimaerin and the mutants with no GAP activity bound Rac1 with similar apparent binding constants. Thus, this mutant analysis allows discrimination between Rac1-binding and Rac1 GTPase- activating residues. | |
dc.source | Scopus | |
dc.type | Article | |
dc.contributor.department | INSTITUTE OF MOLECULAR & CELL BIOLOGY | |
dc.description.sourcetitle | Journal of Biological Chemistry | |
dc.description.volume | 269 | |
dc.description.issue | 26 | |
dc.description.page | 17642-17648 | |
dc.description.coden | JBCHA | |
dc.identifier.isiut | NOT_IN_WOS | |
Appears in Collections: | Staff Publications |
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