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1byv

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[[Image:1byv.gif|left|200px]]<br /><applet load="1byv" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1byv.gif|left|200px]]
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caption="1byv" />
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'''GLYCOSYLATED EEL CALCITONIN'''<br />
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{{Structure
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|PDB= 1byv |SIZE=350|CAPTION= <scene name='initialview01'>1byv</scene>
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> and <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''GLYCOSYLATED EEL CALCITONIN'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1BYV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Anguilla_japonica Anguilla japonica] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BYV OCA].
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1BYV 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].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10387083 10387083]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/10387083 10387083]
[[Category: Anguilla japonica]]
[[Category: Anguilla japonica]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: osteoporosis]]
[[Category: osteoporosis]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:17:39 2008''

Revision as of 08:17, 20 March 2008

Image:1byv.gif


PDB ID 1byv

Drag the structure with the mouse to rotate
Ligands: and
Coordinates: save as pdb, mmCIF, xml



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.

About this Structure

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

Reference

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 Thu Mar 20 10:17:39 2008

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