1xjy
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xjy OCA], [https://pdbe.org/1xjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xjy RCSB], [https://www.ebi.ac.uk/pdbsum/1xjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xjy ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1xjy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1xjy OCA], [https://pdbe.org/1xjy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1xjy RCSB], [https://www.ebi.ac.uk/pdbsum/1xjy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1xjy ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | 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<ref>PMID:15735333</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1xjy" style="background-color:#fffaf0;"></div> | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
The crystal structures of the DNA binding sites of the RUNX1 transcription factor
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