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Int. J. Mol. Sci. 2007, 8(4), 284-294; doi:10.3390/i8040284
Article

Biochemical Analyses of Csx/Nkx2.5 Mutants and Their Structure–Function Relationship

, , , ,  and *
Received: 13 February 2007 / Accepted: 26 March 2007 / Published: 12 April 2007
(This article belongs to the Special Issue Interaction of Biological Molecules)
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Abstract

A homeodomain-containing transcription factor Csx/Nkx2.5 is an importantregulator of cardiogensis in mammals. There has been considerable interest in understandingdeterminants of the diverse cardiac phenotypes associated with Csx/Nkx2.5 mutationssituated within or around the homeodomain in patients. To make clear of the functionalproperties of the regions out of homeodomain, we found that mutants locate outside of thehomeodomain retained intact nuclear localization and have nearly normal or increasedtranscriptional activity but impaired DNA binding capability, the C-terminus region exhibitsan inhibitory function on transcriptional activity of wild type Csx/Nkx2.5, and the NK2-Specific Domain is likely to facilitate both DNA binding and protein-protein interaction. Inthe current study, deletion mutant in homeodomain displayed extremely different biologicalappearance from the mutants with deletion outside of the homeodomain, these may explainthe clinical observation that patients with missense situated outside the homeodomain werenot associated with atrioventricular conduction disturbance.
Keywords: Csx/Nkx2.5; sporadic human congenital heart diseases (CHD); regions out of homeodomain; biochemical characteristics Csx/Nkx2.5; sporadic human congenital heart diseases (CHD); regions out of homeodomain; biochemical characteristics
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Chen, Y.-Z.; Ying, H.; Zhang, J.; Cheng, W.; Kang, Y.-X.; Hua, Z.-C. Biochemical Analyses of Csx/Nkx2.5 Mutants and Their Structure–Function Relationship. Int. J. Mol. Sci. 2007, 8, 284-294.

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