1ljm: Difference between revisions
New page: left|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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[[Image:1ljm.gif|left|200px]]<br /> | [[Image:1ljm.gif|left|200px]]<br /><applet load="1ljm" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1ljm" size=" | |||
caption="1ljm, resolution 2.5Å" /> | caption="1ljm, resolution 2.5Å" /> | ||
'''DNA recognition is mediated by conformational transition and by DNA bending'''<br /> | '''DNA recognition is mediated by conformational transition and by DNA bending'''<br /> | ||
==Overview== | ==Overview== | ||
The Runt domain proteins are transcription regulators of major | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1LJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1LJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LJM OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bartfeld, D.]] | [[Category: Bartfeld, D.]] | ||
[[Category: Couture, G | [[Category: Couture, G C.]] | ||
[[Category: Frolow, F.]] | [[Category: Frolow, F.]] | ||
[[Category: Groner, Y.]] | [[Category: Groner, Y.]] | ||
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[[Category: immunoglobulin fold]] | [[Category: immunoglobulin fold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:30 2008'' | ||
Revision as of 14:45, 21 February 2008
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DNA recognition is mediated by conformational transition and by DNA bending
OverviewOverview
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.
DiseaseDisease
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 StructureAbout this Structure
1LJM is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Thu Feb 21 13:45:30 2008