1ljm
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(New page: 200px<br /> <applet load="1ljm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ljm, resolution 2.5Å" /> '''DNA recognition is m...)
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Revision as of 15:55, 12 November 2007
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DNA recognition is mediated by conformational transition and by DNA bending
Contents |
Overview
The Runt domain proteins are transcription regulators of major, developmental pathways. Here we present the crystal structures of the Runt, domain (RD) of the human protein RUNX1 and its DNA binding site in their, free states and compare them with the published crystal structures of RD, bound to DNA and to the partner protein CBFbeta. We demonstrate that (1), RD undergoes an allosteric transition upon DNA binding, which is further, stabilized by CBFbeta, and that (2) the free DNA target adopts a, bent-helical conformation compatible with that of the complex. These, findings elucidate the mechanism by which CBFbeta enhances RD binding to, DNA as well as the role of the intrinsic conformation of the DNA target in, the recognition process.
Disease
Known diseases associated with this structure: Leukemia, acute myeloid OMIM:[151385], Platelet disorder, familial, with associated myeloid malignancy OMIM:[151385], Rheumatoid arthritis, susceptibility to OMIM:[151385]
About this Structure
1LJM is a Single protein structure of sequence from Homo sapiens with CL as ligand. Full crystallographic information is available from OCA.
Reference
DNA recognition by the RUNX1 transcription factor is mediated by an allosteric transition in the RUNT domain and by DNA bending., Bartfeld D, Shimon L, Couture GC, Rabinovich D, Frolow F, Levanon D, Groner Y, Shakked Z, Structure. 2002 Oct;10(10):1395-407. PMID:12377125
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