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1tfs

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[[Image:1tfs.gif|left|200px]]
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{{STRUCTURE_1tfs| PDB=1tfs | SCENE= }}
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'''NMR AND RESTRAINED MOLECULAR DYNAMICS STUDY OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF TOXIN FS2, A SPECIFIC BLOCKER OF THE L-TYPE CALCIUM CHANNEL, ISOLATED FROM BLACK MAMBA VENOM'''
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===NMR AND RESTRAINED MOLECULAR DYNAMICS STUDY OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF TOXIN FS2, A SPECIFIC BLOCKER OF THE L-TYPE CALCIUM CHANNEL, ISOLATED FROM BLACK MAMBA VENOM===
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==Overview==
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The three-dimensional solution structure of toxin FS2, a 60-residue polypeptide isolated from the venom of black mamba snake (Dendroaspis polylepis polylepis), has been determined by nuclear magnetic resonance spectroscopy. Using 600 NOE constraints and 55 dihedral angle constraints, a set of 20 structures obtained from distance-geometry calculations was further refined by molecular dynamics calculations using a combined simulated annealing-restrained MD protocol. The resulting 20 conformers, taken to represent the solution structure, give an average rmsd of 1.2 A for their backbone atoms, relative to the average structure. The overall resulting three-fingered structure is similar to those already observed in several postsynaptic neurotoxins, cardiotoxins, and fasciculins, which all share with toxin FS2 the same network of four disulfide bridges. The overall concavity of the molecule, considered as a flat bottomed dish, is oriented toward the C-terminal loop of the molecule. This orientation is similar to that of fasciculins and cardiotoxins but opposite to that of neurotoxins. On the basis of the local rms displacements between the 20 conformers, the structure of the first loop appears to be less well defined in FS2 than in the previously reported neurotoxin structures, but fasciculin 1 shows a similar trend with particularly high temperature factors for this part of the X-ray structure. The concave side which presents most of the positively charged residues is quite similar in FS2 and fasciculin 1. The main difference is shown by the convex side of the third loop, mostly hydrophobic in FS2, in contrast to the pair of negatively charged aspartates in fasciculin 1. This difference could be one of the factors leading to the distinct pharmacological properties-L-type calcium channel blocker for FS2 and cholinesterase inhibitor for fasciculin--observed for these two subgroups of the "angusticeps-type" toxins.
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{{ABSTRACT_PUBMED_7727450}}
==About this Structure==
==About this Structure==
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1TFS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFS OCA].
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1TFS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Dendroaspis_polylepis_polylepis Dendroaspis polylepis polylepis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TFS OCA].
==Reference==
==Reference==
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[[Category: Pascaud, F.]]
[[Category: Pascaud, F.]]
[[Category: Toxin]]
[[Category: Toxin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:54:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 22:55:56 2008''

Revision as of 19:56, 27 July 2008

Image:1tfs.png

Template:STRUCTURE 1tfs

NMR AND RESTRAINED MOLECULAR DYNAMICS STUDY OF THE THREE-DIMENSIONAL SOLUTION STRUCTURE OF TOXIN FS2, A SPECIFIC BLOCKER OF THE L-TYPE CALCIUM CHANNEL, ISOLATED FROM BLACK MAMBA VENOM

Template:ABSTRACT PUBMED 7727450

About this Structure

1TFS is a Single protein structure of sequence from Dendroaspis polylepis polylepis. Full experimental information is available from OCA.

Reference

NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom., Albrand JP, Blackledge MJ, Pascaud F, Hollecker M, Marion D, Biochemistry. 1995 May 2;34(17):5923-37. PMID:7727450

Page seeded by OCA on Sun Jul 27 22:55:56 2008

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