121d: 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=121d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=121d OCA], [https://pdbe.org/121d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=121d RCSB], [https://www.ebi.ac.uk/pdbsum/121d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=121d ProSAT]</span></td></tr>
 </table>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The molecular structure of the complex between the minor groove binding drug netropsin and the dodecamer d(CGCAAATTTGCG) has been solved and refined by X-ray diffraction analysis to an R-factor of 19.8% and 2.2-A resolution. The drug lies in the narrow minor groove of the B-DNA fragment, covering five of the six A.T base pairs (from A5.T20 to T9.A16). The long six A.T base pair tract allows the drug to bind in a position that optimizes its contacts with the DNA, establishing hydrogen bonds with O2 of thymines and N3 of adenines. The DNA molecule shows a high propeller twist only at the A6.T19 step of the A-tract. Two three-centered hydrogen bonds are observed in the major groove at half of the A-tract.
-Molecular structure of the A-tract DNA dodecamer d(CGCAAATTTGCG) complexed with the minor groove binding drug netropsin.,Tabernero L, Verdaguer N, Coll M, Fita I, van der Marel GA, van Boom JH, Rich A, Aymami J Biochemistry. 1993 Aug 24;32(33):8403-10. PMID:8395202<ref>PMID:8395202</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 121d" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
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 </StructureSection>