1ljm
From Proteopedia
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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. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: Leukemia, acute myeloid OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=151385 151385]], Platelet disorder, familial, with associated myeloid malignancy OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=151385 151385]], Rheumatoid arthritis, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=151385 151385]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Shakked, Z.]] | [[Category: Shakked, Z.]] | ||
[[Category: Shimon, L.]] | [[Category: Shimon, L.]] | ||
| - | [[Category: CL]] | ||
[[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'' |
Revision as of 19:03, 30 March 2008
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Gene: | human (Homo sapiens) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
DNA recognition is mediated by conformational transition and by DNA bending
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.
About this Structure
1LJM is a Single protein structure of sequence from Homo sapiens. 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
Page seeded by OCA on Sun Mar 30 22:03:32 2008
