1ljm: Difference between revisions
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|PDB= 1ljm |SIZE=350|CAPTION= <scene name='initialview01'>1ljm</scene>, resolution 2.5Å | |PDB= 1ljm |SIZE=350|CAPTION= <scene name='initialview01'>1ljm</scene>, resolution 2.5Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene> | |LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= human ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |GENE= human ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ljm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ljm OCA], [http://www.ebi.ac.uk/pdbsum/1ljm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ljm RCSB]</span> | |||
}} | }} | ||
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==Overview== | ==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. | 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. | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Shakked, Z.]] | [[Category: Shakked, Z.]] | ||
[[Category: Shimon, L.]] | [[Category: Shimon, L.]] | ||
[[Category: beta-sandwich]] | [[Category: beta-sandwich]] | ||
[[Category: immunoglobulin fold]] | [[Category: immunoglobulin fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:03:32 2008'' | ||