1xjy
From Proteopedia
(New page: 200px<br /><applet load="1xjy" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xjy, resolution 2.00Å" /> '''The crystal structur...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1xjy.gif|left|200px]]<br /><applet load="1xjy" size=" | + | [[Image:1xjy.gif|left|200px]]<br /><applet load="1xjy" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1xjy, resolution 2.00Å" /> | caption="1xjy, resolution 2.00Å" /> | ||
'''The crystal structures of the DNA binding sites of the RUNX1 transcription factor'''<br /> | '''The crystal structures of the DNA binding sites of the RUNX1 transcription factor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Runt-domain (RD) proteins are transcription factors that play fundamental | + | Runt-domain (RD) proteins are transcription factors that play fundamental roles in various developmental pathways. They bind specifically to DNA sequences of the general form PyGPyGGTPy (Py = pyrimidine), through which they regulate transcription of target genes. The DNA duplex TCTGCGGTC/TGACCGCAG, incorporating the binding site for the RD transcription factors (bold), was crystallized in space group P4(3). X-ray analysis of two crystals diffracting to 1.7 and 2.0 angstroms resolution, which had slight variations in their unit-cell parameters, revealed two distinct conformations of the A-DNA helix. The two crystal structures possessed several structure and hydration features that had previously been observed in A-DNA duplexes. A comparative analysis of the present A-DNA structures and those of previously reported B-DNA crystal structures of RD-binding sites in free and protein-bound states showed the various duplexes to display several common features. Within this series, the present A-DNA duplexes adopt two conformations along the pathway from the canonical A-DNA to the B-DNA forms and the protein-bound helices display conformational features that are intermediate between those of the current A-DNA structures and that of the B-DNA-type helix of the free RD target. Based on these data and energy considerations, it is likely that the propensity of the RD-binding site to adopt the A-DNA or B-DNA conformation in solution depends on the sequence context and environmental conditions, and that the transition from either DNA form to the protein-bound conformation involves a small energy barrier. |
==About this Structure== | ==About this Structure== | ||
| - | 1XJY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1XJY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XJY OCA]. |
==Reference== | ==Reference== | ||
| Line 21: | Line 21: | ||
[[Category: runx1]] | [[Category: runx1]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:55:34 2008'' |
Revision as of 13:55, 21 February 2008
|
The crystal structures of the DNA binding sites of the RUNX1 transcription factor
Overview
Runt-domain (RD) proteins are transcription factors that play fundamental roles in various developmental pathways. They bind specifically to DNA sequences of the general form PyGPyGGTPy (Py = pyrimidine), through which they regulate transcription of target genes. The DNA duplex TCTGCGGTC/TGACCGCAG, incorporating the binding site for the RD transcription factors (bold), was crystallized in space group P4(3). X-ray analysis of two crystals diffracting to 1.7 and 2.0 angstroms resolution, which had slight variations in their unit-cell parameters, revealed two distinct conformations of the A-DNA helix. The two crystal structures possessed several structure and hydration features that had previously been observed in A-DNA duplexes. A comparative analysis of the present A-DNA structures and those of previously reported B-DNA crystal structures of RD-binding sites in free and protein-bound states showed the various duplexes to display several common features. Within this series, the present A-DNA duplexes adopt two conformations along the pathway from the canonical A-DNA to the B-DNA forms and the protein-bound helices display conformational features that are intermediate between those of the current A-DNA structures and that of the B-DNA-type helix of the free RD target. Based on these data and energy considerations, it is likely that the propensity of the RD-binding site to adopt the A-DNA or B-DNA conformation in solution depends on the sequence context and environmental conditions, and that the transition from either DNA form to the protein-bound conformation involves a small energy barrier.
About this Structure
1XJY is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.
Reference
Structures of the DNA-binding site of Runt-domain transcription regulators., Kitayner M, Rozenberg H, Rabinovich D, Shakked Z, Acta Crystallogr D Biol Crystallogr. 2005 Mar;61(Pt 3):236-46. Epub 2005, Feb 24. PMID:15735333
Page seeded by OCA on Thu Feb 21 15:55:34 2008
