1bah: Difference between revisions

Revision as of 18:42, 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:1bah.png

Template:STRUCTURE 1bah

A TWO DISULFIDE DERIVATIVE OF CHARYBDOTOXIN WITH DISULFIDE 13-33 REPLACED BY TWO ALPHA-AMINOBUTYRIC ACIDS, NMR, 30 STRUCTURESA TWO DISULFIDE DERIVATIVE OF CHARYBDOTOXIN WITH DISULFIDE 13-33 REPLACED BY TWO ALPHA-AMINOBUTYRIC ACIDS, NMR, 30 STRUCTURES

Template:ABSTRACT PUBMED 9092804

About this StructureAbout this Structure

1BAH is a Single protein structure of sequence from Leiurus quinquestriatus. Full experimental information is available from OCA.

ReferenceReference

NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing., Song J, Gilquin B, Jamin N, Drakopoulou E, Guenneugues M, Dauplais M, Vita C, Menez A, Biochemistry. 1997 Apr 1;36(13):3760-6. PMID:9092804

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

OCA

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-[[Image:1bah.gif|left|200px]]
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-'''A TWO DISULFIDE DERIVATIVE OF CHARYBDOTOXIN WITH DISULFIDE 13-33 REPLACED BY TWO ALPHA-AMINOBUTYRIC ACIDS, NMR, 30 STRUCTURES'''
+===A TWO DISULFIDE DERIVATIVE OF CHARYBDOTOXIN WITH DISULFIDE 13-33 REPLACED BY TWO ALPHA-AMINOBUTYRIC ACIDS, NMR, 30 STRUCTURES===
-==Overview==
+<!--
-The alpha/beta scorpion fold consisting of a short alpha-helix and beta-sheet is a structural motif common to scorpion toxins, insect defensins, and plant gamma-thionins that invariably contains three disulfides. CHABII is a two-disulfide derivative of the scorpion toxin charybdotoxin (ChTX), chemically synthesized by inserting two L-alpha-aminobutyric acids in place of the two half-cystine residues involved in the disulfide 13-33. This disulfide is one of the two disulfides which connect the alpha-helix to the beta-sheet. The solution structure of CHABII was determined at pH 6.3 and 5 degrees C using 2D NMR and simulated annealing from 513 distance and 46 dihedral angle constraints. The NMR structure of CHABII is well-defined as judged from the low value of the averaged backbone rms deviation between the 30 lowest energy structures and the energy-minimized mean structure ((rmsd) = 0.65 A for the entire sequence and 0.48 A for the segment 3-36). Analysis and comparison of the solution structures of CHABII and ChTX lead to the following conclusions: (i) the fold of CHABII is similar to that of ChTX as indicated by the low value of the averaged backbone atomic rms deviation between the 10 lowest energy solution structures of the two proteins (1.44 A); (ii) the packing of the hydrophobic core is well-preserved, underlying the critical structural role of the hydrophobic interactions even for such a small and cysteine-rich protein as ChTX.
+The line below this paragraph, {{ABSTRACT_PUBMED_9092804}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 9092804 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_9092804}}
 ==About this Structure==
-BAH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Leiurus_quinquestriatus Leiurus quinquestriatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAH OCA].
+BAH is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Leiurus_quinquestriatus Leiurus quinquestriatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BAH OCA].
 ==Reference==
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 [[Category: Potassium channel inhibitor]]
 [[Category: Toxin]]
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