1byv: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1byv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anguilla_japonica Anguilla japonica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BYV FirstGlance]. <br> | <table><tr><td colspan='2'>[[1byv]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Anguilla_japonica Anguilla japonica]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYV OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BYV FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>< | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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> | <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=1byv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1byv RCSB], [http://www.ebi.ac.uk/pdbsum/1byv 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=1byv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1byv OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1byv RCSB], [http://www.ebi.ac.uk/pdbsum/1byv PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 30: | Line 30: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Anguilla japonica]] | [[Category: Anguilla japonica]] | ||
[[Category: Haneda, K | [[Category: Haneda, K]] | ||
[[Category: Hashimoto, Y | [[Category: Hashimoto, Y]] | ||
[[Category: Inazu, T | [[Category: Inazu, T]] | ||
[[Category: Nishikido, J | [[Category: Nishikido, J]] | ||
[[Category: Opella, S J | [[Category: Opella, S J]] | ||
[[Category: Toma, K | [[Category: Toma, K]] | ||
[[Category: Valentine, K G | [[Category: Valentine, K G]] | ||
[[Category: Yamamoto, K | [[Category: Yamamoto, K]] | ||
[[Category: Calcium-regulator]] | [[Category: Calcium-regulator]] | ||
[[Category: Hormone-growth factor complex]] | [[Category: Hormone-growth factor complex]] | ||
[[Category: Horomone]] | [[Category: Horomone]] | ||
[[Category: Osteoporosis]] | [[Category: Osteoporosis]] | ||
Revision as of 15:09, 22 December 2014
GLYCOSYLATED EEL CALCITONINGLYCOSYLATED EEL CALCITONIN
Structural highlights
Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe three-dimensional structures of eel calcitonin (CT) and two glycosylated CT derivatives, [Asn(GlcNAc)3]-CT (CT-GlcNAc) and [Asn(Man6-GlcNAc2)3]-CT (CT-M6), in micelles were determined by solution NMR spectroscopy. The topologies of these peptides associated with oriented lipid bilayers were determined with solid-state NMR. All of the peptides were found to have an identical conformation in micelles characterized by an amphipathic alpha-helix consisting of residues Ser5 through Leu19 followed by an unstructured region at the C-terminus. The overall conformation of the peptide moiety was not affected by the glycosylation. Nevertheless, comparison of the relative exchange rates of the Leu12 amide proton might suggest the possibility that fluctuations of the alpha-helix are reduced by glycosylation. The presence of NOEs between the carbohydrate and the peptide moieties of CT-GlcNAc and CT-M6 and the amide proton chemical shift data suggested that the carbohydrate interacted with the peptide, and this might account for the conformational stabilization of the alpha-helix. Both the unmodified CT and the glycosylated CT were found to have orientations with their helix axes parallel to the plane of the lipid bilayers by solid-state NMR spectroscopy. Effects of glycosylation on the structure and dynamics of eel calcitonin in micelles and lipid bilayers determined by nuclear magnetic resonance spectroscopy.,Hashimoto Y, Toma K, Nishikido J, Yamamoto K, Haneda K, Inazu T, Valentine KG, Opella SJ Biochemistry. 1999 Jun 29;38(26):8377-84. PMID:10387083[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
| ||||||||||||||||||