1ug4

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(New page: 200px<br /><applet load="1ug4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ug4, resolution 1.6&Aring;" /> '''Crystal Structure of ...)
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[[Image:1ug4.gif|left|200px]]<br /><applet load="1ug4" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1ug4, resolution 1.6&Aring;" />
caption="1ug4, resolution 1.6&Aring;" />
'''Crystal Structure of Cardiotoxin VI from Taiwan Cobra (Naja atra) Venom'''<br />
'''Crystal Structure of Cardiotoxin VI from Taiwan Cobra (Naja atra) Venom'''<br />
==Overview==
==Overview==
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Natural homologues of cobra cardiotoxins (CTXs) were classified into two, structural subclasses of group I and II based on the amino acid sequence, and circular dichroism analysis, but the exact differences in their, three-dimensional structures and biological significance remain elusive., We show by circular dichroism, NMR spectroscopic, and X-ray, crystallographic analyses of a newly purified group I CTX A6 from eastern, Taiwan cobra (Naja atra) venoms that its loop I conformation adopts a type, VIa turn with a cis peptide bond located between two proline residues of, PPxY. A similar "banana-twisted" conformation can be observed in other, group I CTXs and also in cyclolinopeptide A and its analogues. By binding, to the membrane environment, group I CTX undergoes a conformational change, to adopt a more extended hydrophobic domain with beta-sheet twisting, closer to the one adopted by group II CTX. This result resolves a, discrepancy in the CTX structural difference reported previously between, solution as well as crystal state and shows that, in addition to the, hydrophobicity, the exact loop I conformation also plays an important role, in CTX-membrane interaction. Potential protein targets of group I CTXs, after cell internalization are also discussed on the basis of the, determined loop I conformation.
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Natural homologues of cobra cardiotoxins (CTXs) were classified into two structural subclasses of group I and II based on the amino acid sequence and circular dichroism analysis, but the exact differences in their three-dimensional structures and biological significance remain elusive. We show by circular dichroism, NMR spectroscopic, and X-ray crystallographic analyses of a newly purified group I CTX A6 from eastern Taiwan cobra (Naja atra) venoms that its loop I conformation adopts a type VIa turn with a cis peptide bond located between two proline residues of PPxY. A similar "banana-twisted" conformation can be observed in other group I CTXs and also in cyclolinopeptide A and its analogues. By binding to the membrane environment, group I CTX undergoes a conformational change to adopt a more extended hydrophobic domain with beta-sheet twisting closer to the one adopted by group II CTX. This result resolves a discrepancy in the CTX structural difference reported previously between solution as well as crystal state and shows that, in addition to the hydrophobicity, the exact loop I conformation also plays an important role in CTX-membrane interaction. Potential protein targets of group I CTXs after cell internalization are also discussed on the basis of the determined loop I conformation.
==About this Structure==
==About this Structure==
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1UG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UG4 OCA].
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1UG4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Naja_atra Naja atra]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UG4 OCA].
==Reference==
==Reference==
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[[Category: Naja atra]]
[[Category: Naja atra]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chen, C.J.]]
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[[Category: Chen, C J.]]
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[[Category: Chung, F.Y.]]
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[[Category: Chung, F Y.]]
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[[Category: Wu, W.G.]]
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[[Category: Wu, W G.]]
[[Category: cardiotoxin]]
[[Category: cardiotoxin]]
[[Category: cobra]]
[[Category: cobra]]
[[Category: venom]]
[[Category: venom]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:05:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:12 2008''

Revision as of 13:24, 21 February 2008


1ug4, resolution 1.6Å

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Crystal Structure of Cardiotoxin VI from Taiwan Cobra (Naja atra) Venom

Overview

Natural homologues of cobra cardiotoxins (CTXs) were classified into two structural subclasses of group I and II based on the amino acid sequence and circular dichroism analysis, but the exact differences in their three-dimensional structures and biological significance remain elusive. We show by circular dichroism, NMR spectroscopic, and X-ray crystallographic analyses of a newly purified group I CTX A6 from eastern Taiwan cobra (Naja atra) venoms that its loop I conformation adopts a type VIa turn with a cis peptide bond located between two proline residues of PPxY. A similar "banana-twisted" conformation can be observed in other group I CTXs and also in cyclolinopeptide A and its analogues. By binding to the membrane environment, group I CTX undergoes a conformational change to adopt a more extended hydrophobic domain with beta-sheet twisting closer to the one adopted by group II CTX. This result resolves a discrepancy in the CTX structural difference reported previously between solution as well as crystal state and shows that, in addition to the hydrophobicity, the exact loop I conformation also plays an important role in CTX-membrane interaction. Potential protein targets of group I CTXs after cell internalization are also discussed on the basis of the determined loop I conformation.

About this Structure

1UG4 is a Single protein structure of sequence from Naja atra. Full crystallographic information is available from OCA.

Reference

Structural difference between group I and group II cobra cardiotoxins: X-ray, NMR, and CD analysis of the effect of cis-proline conformation on three-fingered toxins., Chen TS, Chung FY, Tjong SC, Goh KS, Huang WN, Chien KY, Wu PL, Lin HC, Chen CJ, Wu WG, Biochemistry. 2005 May 24;44(20):7414-26. PMID:15895985

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