1byv: Difference between revisions

Revision as of 19:58, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1byv.png

Template:STRUCTURE 1byv

GLYCOSYLATED EEL CALCITONINGLYCOSYLATED EEL CALCITONIN

Template:ABSTRACT PUBMED 10387083

About this StructureAbout this Structure

1BYV is a Single protein structure of sequence from Anguilla japonica. Full experimental information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Mon Jun 30 19:58:04 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1byv.gif|left|200px]]
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 {{STRUCTURE_1byv|  PDB=1byv  |  SCENE=  }}
-'''GLYCOSYLATED EEL CALCITONIN'''
+===GLYCOSYLATED EEL CALCITONIN===
-==Overview==
+<!--
-The 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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10387083}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10387083 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10387083}}
 ==About this Structure==
-BYV is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Anguilla_japonica Anguilla japonica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYV OCA].
+BYV is a [[Single protein]] structure of 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].
 ==Reference==
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 [[Category: Horomone]]
 [[Category: Osteoporosis]]
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