1dw5: Difference between revisions

Revision as of 23:42, 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:1dw5.png

Template:STRUCTURE 1dw5

NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGESNMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGES

Template:ABSTRACT PUBMED 10747778

About this StructureAbout this Structure

1DW5 is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

Structural and dynamic characterization of omega-conotoxin MVIIA: the binding loop exhibits slow conformational exchange., Atkinson RA, Kieffer B, Dejaegere A, Sirockin F, Lefevre JF, Biochemistry. 2000 Apr 11;39(14):3908-19. PMID:10747778

Page seeded by OCA on Mon Jun 30 23:42:35 2008

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

OCA

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-[[Image:1dw5.gif|left|200px]]
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 {{STRUCTURE_1dw5|  PDB=1dw5  |  SCENE=  }}
-'''NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGES'''
+===NMR STRUCTURE OF OMEGA-CONOTOXIN MVIIA: NO CONSTRAINTS ON DISULPHIDE BRIDGES===
-==Overview==
+<!--
-omega-Conotoxin MVIIA is a 25-residue, disulfide-bridged polypeptide from the venom of the sea snail Conus magus that binds to neuronal N-type calcium channels. It forms a compact folded structure, presenting a loop between Cys8 and Cys15 that contains a set of residues critical for its binding. The loop does not have a unique defined structure, nor is it intrinsically flexible. Broadening of a subset of resonances in the NMR spectrum at low temperature, anomalous temperature dependence of the chemical shifts of some resonances, and exchange contributions to J(0) from (13)C relaxation measurements reveal that conformational exchange affects the residues in this loop. The effects of this exchange on the calculated structure of omega-conotoxin MVIIA are discussed. The exchange appears to be associated with a change in the conformation of the disulfide bridge Cys8-Cys20. The implications for the use of the omega-conotoxins as a scaffold for carrying other functions is discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_10747778}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10747778 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10747778}}
 ==About this Structure==
-DW5 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DW5 OCA].
+DW5 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DW5 OCA].
 ==Reference==
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 [[Category: Conformational exchange]]
 [[Category: Conotoxin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 14:21:18 2008''
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