This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1afz

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 04:51, 10 September 2015

SOLUTION NMR STRUCTURE OF AN 11 BASE-PAIR OLIGONUCLEOTIDE FROM THE HUMAN N-RAS PROTOONCOGENE ENCODING FOR AMINO ACIDS 11-13 OF P21, MINIMIZED AVERAGE STRUCTURE

Structural highlights

1afz is a 2 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1af1
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Publication Abstract from PubMed

The structure of d(GGCAGGTGGTG).d(CACCACCTGCC), consisting of codons 11, 12 (underlined), and 13 of the human n-ras protooncogene, was refined from 1H NMR data. Patterns of internucleotide NOEs consistent with a B-form helix were observed for each strand. NOE intensities between purine H8 and H1' protons were small compared to intensities between cytosine H5 and H6 protons, indicative of glycosyl torsion angles in the anti range. Cross-peaks were observed between purine H8 and pyrimidine H5 and CH3 protons on adjacent bases in the direction of purine (5'-->3')pyrimidine, but not in the direction pyrimidine(5'-->3')purine. Watson-Crick hydrogen bonding between bases was intact. A total of 232 experimental distance restraints were obtained. Of these, 143 were intra-residue restraints and 89 were inter-residue restraints. A restrained molecular dynamics/simulated annealing approach yielded 6 MD structures calculated from a B-form starting structure and 6 MD structures from an A-form starting structure. These refined to an average pairwise rms difference of 0.92 angstrom, with maximum pairwise rmsd of 1.35 angstroms. Accuracy of emergent structures was assessed by relaxation matrix back-calculation. The sixth-root residual index of 7.0 x 10(-2) measured between the refined structures and the NOE intensity data suggested that the former were in reasonable agreement with the NOE data. The refined solution structures were in the B-family. Similar to the human n-ras codon 61 sequence [Feng, B., & Stone, M.P. (1995) Chem. Res. Toxicol. 8, 821-832], the ras12 sequence contained local variations in B-like conformation which did not confer large structural alterations upon the duplex, but perhaps modulated the reactivity of the first as compared to the second guanine in codon 12.

Solution structure of an oligodeoxynucleotide containing the human N-ras codon 12 sequence refined from 1H NMR using molecular dynamics restrained by nuclear Overhauser effects.,Zegar IS, Stone MP Chem Res Toxicol. 1996 Jan-Feb;9(1):114-25. PMID:8924579^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Zegar IS, Stone MP. Solution structure of an oligodeoxynucleotide containing the human N-ras codon 12 sequence refined from 1H NMR using molecular dynamics restrained by nuclear Overhauser effects. Chem Res Toxicol. 1996 Jan-Feb;9(1):114-25. PMID:8924579 doi:10.1021/tx9500787

1 Structural highlights
2 Publication Abstract from PubMed
3 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1afz"

@@ Line 4: / Line 4: @@
 <table><tr><td colspan='2'>[[1afz]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AFZ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AFZ FirstGlance]. <br>
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1af1|1af1]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1afz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afz OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1afz RCSB], [http://www.ebi.ac.uk/pdbsum/1afz PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1afz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1afz OCA], [http://pdbe.org/1afz PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1afz RCSB], [http://www.ebi.ac.uk/pdbsum/1afz PDBsum]</span></td></tr>
 </table>
 <div style="background-color:#fffaf0;">
@@ Line 14: / Line 14: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1afz" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1afz

From Proteopedia

Revision as of 04:51, 10 September 2015

SOLUTION NMR STRUCTURE OF AN 11 BASE-PAIR OLIGONUCLEOTIDE FROM THE HUMAN N-RAS PROTOONCOGENE ENCODING FOR AMINO ACIDS 11-13 OF P21, MINIMIZED AVERAGE STRUCTURE

Structural highlights

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox