1cmr: Difference between revisions

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[[Image:1cmr.gif|left|200px]]
{{Seed}}
[[Image:1cmr.png|left|200px]]


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{{STRUCTURE_1cmr|  PDB=1cmr  |  SCENE=  }}  
{{STRUCTURE_1cmr|  PDB=1cmr  |  SCENE=  }}  


'''NMR SOLUTION STRUCTURE OF A CHIMERIC PROTEIN, DESIGNED BY TRANSFERRING A FUNCTIONAL SNAKE BETA-HAIRPIN INTO A SCORPION ALPHA/BETA SCAFFOLD (PH 3.5, 20C), NMR, 18 STRUCTURES'''
===NMR SOLUTION STRUCTURE OF A CHIMERIC PROTEIN, DESIGNED BY TRANSFERRING A FUNCTIONAL SNAKE BETA-HAIRPIN INTO A SCORPION ALPHA/BETA SCAFFOLD (PH 3.5, 20C), NMR, 18 STRUCTURES===




==Overview==
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The alpha/beta scorpion fold is shared by scorpion toxins, insect defensins, and plant thionins. This small and functionally versatile template contains an alpha-helix and a triple beta-sheet linked by three disulfide bridges. With the view to introduce novel functional centers within this fold, we replaced the sequence (the cysteines and glycines excepted) of the original beta-hairpin of a scorpion toxin by the sequence of a beta-hairpin that forms part of the site by which snake neurotoxins bind to nicotinic acetylcholine receptors (AcChOR). The resulting chimeric protein, synthesized by chemical means, binds to AcChOR, though with a lower affinity than the snake toxins [Drakopoulou; E., Zinn-Justin, S., Guenneugues, M., Gilquin, B., Menez, A., &amp; Vita, C. (1996) J. Biol. Chem. 271, 11979-11987]. The work described in this paper is an attempt to clarify the structural consequences associated with the transfer of the beta-hairpin. We report the determination of the three-dimensional solution structure of the chimeric protein by proton NMR spectroscopy and molecular dynamics calculations. Comparison of the structure of the chimera with those of the scorpion alpha/beta toxin and of the snake neurotoxin shows that (i) the new protein folds as an alpha/beta motif and (ii) the beta-hairpins of the chimera and of the curaremimetic toxin adopt a similar conformation. A closer inspection of the differences between the structures of the original and transferred beta-hairpins allows rationalization of the biological properties of the chimera.
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{{ABSTRACT_PUBMED_8679614}}


==About this Structure==
==About this Structure==
1CMR is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMR OCA].  
1CMR is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CMR OCA].  


==Reference==
==Reference==
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[[Category: Antagonist of nicotinic acetylcholine receptor]]
[[Category: Antagonist of nicotinic acetylcholine receptor]]
[[Category: Curaremimetic protein]]
[[Category: Curaremimetic protein]]
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Revision as of 17:57, 30 June 2008

File:1cmr.png

Template:STRUCTURE 1cmr

NMR SOLUTION STRUCTURE OF A CHIMERIC PROTEIN, DESIGNED BY TRANSFERRING A FUNCTIONAL SNAKE BETA-HAIRPIN INTO A SCORPION ALPHA/BETA SCAFFOLD (PH 3.5, 20C), NMR, 18 STRUCTURES

Template:ABSTRACT PUBMED 8679614

About this Structure

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

Reference

Transfer of a beta-hairpin from the functional site of snake curaremimetic toxins to the alpha/beta scaffold of scorpion toxins: three-dimensional solution structure of the chimeric protein., Zinn-Justin S, Guenneugues M, Drakopoulou E, Gilquin B, Vita C, Menez A, Biochemistry. 1996 Jul 2;35(26):8535-43. PMID:8679614

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