2ctx

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(New page: 200px<br /><applet load="2ctx" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ctx, resolution 2.4&Aring;" /> '''THE REFINED CRYSTAL S...)
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[[Image:2ctx.jpg|left|200px]]<br /><applet load="2ctx" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ctx.jpg|left|200px]]<br /><applet load="2ctx" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2ctx, resolution 2.4&Aring;" />
caption="2ctx, resolution 2.4&Aring;" />
'''THE REFINED CRYSTAL STRUCTURE OF ALPHA-COBRATOXIN FROM NAJA NAJA SIAMENSIS AT 2.4-ANGSTROMS RESOLUTION'''<br />
'''THE REFINED CRYSTAL STRUCTURE OF ALPHA-COBRATOXIN FROM NAJA NAJA SIAMENSIS AT 2.4-ANGSTROMS RESOLUTION'''<br />
==Overview==
==Overview==
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The crystal structure of the "long" alpha-neurotoxin alpha-cobratoxin was, refined to an R-factor of 19.5% using 3271 x-ray data to 2.4-A resolution., The polypeptide chain forms three loops, I, II, III, knotted together by, four disulfide bridges, with the most prominent, loop II, containing, another disulfide close to its lower tip. Loop I is stabilized by one, beta-turn and two beta-sheet hydrogen bonds; loop II by eight beta-sheet, hydrogen bonds, with the tip folded into two distorted right-handed, helical turns stabilized by two alpha-helical and two beta-turn hydrogen, bonds; and loop III by hydrophobic interactions and one beta-turn. Loop II, and one strand of loop III form an antiparallel triple-pleated beta-sheet, and tight anchoring of the Asn63 side chain fixes the tail segment. In the, crystal lattice, the alpha-cobratoxin molecules dimerize by beta-sheet, formation between strands 53 and 57 of symmetry-related molecules. Because, such interactions are found also in a cardiotoxin and alpha-bungarotoxin, this could be of importance for interaction with acetylcholine receptor.
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The crystal structure of the "long" alpha-neurotoxin alpha-cobratoxin was refined to an R-factor of 19.5% using 3271 x-ray data to 2.4-A resolution. The polypeptide chain forms three loops, I, II, III, knotted together by four disulfide bridges, with the most prominent, loop II, containing another disulfide close to its lower tip. Loop I is stabilized by one beta-turn and two beta-sheet hydrogen bonds; loop II by eight beta-sheet hydrogen bonds, with the tip folded into two distorted right-handed helical turns stabilized by two alpha-helical and two beta-turn hydrogen bonds; and loop III by hydrophobic interactions and one beta-turn. Loop II and one strand of loop III form an antiparallel triple-pleated beta-sheet, and tight anchoring of the Asn63 side chain fixes the tail segment. In the crystal lattice, the alpha-cobratoxin molecules dimerize by beta-sheet formation between strands 53 and 57 of symmetry-related molecules. Because such interactions are found also in a cardiotoxin and alpha-bungarotoxin, this could be of importance for interaction with acetylcholine receptor.
==About this Structure==
==About this Structure==
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2CTX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_naja Naja naja]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2CTX OCA].
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2CTX is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_naja Naja naja]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CTX OCA].
==Reference==
==Reference==
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[[Category: Lange, G.]]
[[Category: Lange, G.]]
[[Category: Maelicke, A.]]
[[Category: Maelicke, A.]]
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[[Category: Pal, G.P.]]
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[[Category: Pal, G P.]]
[[Category: Saenger, W.]]
[[Category: Saenger, W.]]
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[[Category: Wilson, K.S.]]
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[[Category: Wilson, K S.]]
[[Category: neurotoxin]]
[[Category: neurotoxin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:15:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:52:30 2008''

Revision as of 14:52, 21 February 2008


2ctx, resolution 2.4Å

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THE REFINED CRYSTAL STRUCTURE OF ALPHA-COBRATOXIN FROM NAJA NAJA SIAMENSIS AT 2.4-ANGSTROMS RESOLUTION

Overview

The crystal structure of the "long" alpha-neurotoxin alpha-cobratoxin was refined to an R-factor of 19.5% using 3271 x-ray data to 2.4-A resolution. The polypeptide chain forms three loops, I, II, III, knotted together by four disulfide bridges, with the most prominent, loop II, containing another disulfide close to its lower tip. Loop I is stabilized by one beta-turn and two beta-sheet hydrogen bonds; loop II by eight beta-sheet hydrogen bonds, with the tip folded into two distorted right-handed helical turns stabilized by two alpha-helical and two beta-turn hydrogen bonds; and loop III by hydrophobic interactions and one beta-turn. Loop II and one strand of loop III form an antiparallel triple-pleated beta-sheet, and tight anchoring of the Asn63 side chain fixes the tail segment. In the crystal lattice, the alpha-cobratoxin molecules dimerize by beta-sheet formation between strands 53 and 57 of symmetry-related molecules. Because such interactions are found also in a cardiotoxin and alpha-bungarotoxin, this could be of importance for interaction with acetylcholine receptor.

About this Structure

2CTX is a Single protein structure of sequence from Naja naja. Full crystallographic information is available from OCA.

Reference

The refined crystal structure of alpha-cobratoxin from Naja naja siamensis at 2.4-A resolution., Betzel C, Lange G, Pal GP, Wilson KS, Maelicke A, Saenger W, J Biol Chem. 1991 Nov 15;266(32):21530-6. PMID:1939183

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