1ter: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ter]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TER FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ter]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TER OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1TER FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ter OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ter RCSB], [http://www.ebi.ac.uk/pdbsum/1ter 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=1ter FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ter OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ter RCSB], [http://www.ebi.ac.uk/pdbsum/1ter PDBsum]</span></td></tr> | ||
<table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Apis mellifera]] | [[Category: Apis mellifera]] | ||
[[Category: Nelson, J W | [[Category: Nelson, J W]] | ||
[[Category: Xu, X | [[Category: Xu, X]] | ||
[[Category: Toxin]] | [[Category: Toxin]] | ||
Revision as of 08:43, 22 December 2014
SOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRYSOLUTION STRUCTURE OF TERTIAPIN DETERMINED USING NUCLEAR MAGNETIC RESONANCE AND DISTANCE GEOMETRY
Structural highlights
Publication Abstract from PubMedThe solution structure of tertiapin, a 21-residue bee venom peptide, has been characterized by circular dichroism (CD), two-dimensional nuclear magnetic resonance (NMR) spectroscopy, and distance geometry. A total of 21 lowest error structures were obtained from distance geometry calculations. Superimposition of these structures shows that the backbone of tertiapin is very well defined. One type-I reverse turn from residue 4 to 7 and an alpha-helix from residue 12 to 19 exist in the structure of tertiapin. The alpha-helical region is best defined from both conformational analysis and structural superimposition. The overall three-dimensional structure of tertiapin is highly compact resulting from side chain interactions. The structural information obtained from CD and NMR are compared for both tertiapin and apamin (ref. 3), another bee venom peptide. Tertiapin and apamin have some similar secondary structure, but display different tertiary structures. Solution structure of tertiapin determined using nuclear magnetic resonance and distance geometry.,Xu X, Nelson JW Proteins. 1993 Oct;17(2):124-37. PMID:8265561[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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