1bzb: Difference between revisions
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[[Image:1bzb.gif|left|200px]] | [[Image:1bzb.gif|left|200px]] | ||
'''GLYCOSYLATED EEL CALCITONIN''' | {{Structure | ||
|PDB= 1bzb |SIZE=350|CAPTION= <scene name='initialview01'>1bzb</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''GLYCOSYLATED EEL CALCITONIN''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BZB is a [ | 1BZB is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BZB OCA]. | ||
==Reference== | ==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:[http:// | 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: Single protein]] | [[Category: Single protein]] | ||
[[Category: Haneda, K.]] | [[Category: Haneda, K.]] | ||
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[[Category: osteoporosis]] | [[Category: osteoporosis]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:17:49 2008'' | ||
Revision as of 11:17, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
GLYCOSYLATED EEL CALCITONIN
OverviewOverview
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 StructureAbout this Structure
1BZB is a Single protein structure of sequence from [1]. Full crystallographic 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
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