2crd
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(New page: 200px<br /> <applet load="2crd" size="450" color="white" frame="true" align="right" spinBox="true" caption="2crd" /> '''ANALYSIS OF SIDE-CHAIN ORGANIZATION ON A RE...)
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Revision as of 07:01, 18 November 2007
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ANALYSIS OF SIDE-CHAIN ORGANIZATION ON A REFINED MODEL OF CHARYBDOTOXIN: STRUCTURAL AND FUNCTIONAL IMPLICATIONS
Overview
The spatial organization of side chains on a refined model of, charybdotoxin is presented. First, the structural role of two groups of, well-defined, low-accessible side chains (Thr3, Val5, Val16, Leu20, Cys33, and Leu20, His21, Thr23, Cys17, Cys35) is discussed. These side chains are, conserved in three out of the five known scorpion toxins acting on K+, channels. Interestingly, they are not conserved in scyllatoxin which, presents a slightly different secondary structure organization. Second, the spatial organization of all positively charged residues is analyzed., Comparison with the results presented by Park and Miller [(1992), Biochemistry (preceding paper in this issue)] shows that all functionally, important positive residues are located on the beta-sheet side of the, toxin. These results are different from those obtained by Auguste et al., [(1992) Biochemistry 31, 648-654] on scyllatoxin, which blocks a different, type of K+ channel. This study shows, in fact, that functionally important, positive residues are located on the helix side of the toxin. Thus, charybdotoxin and scyllatoxin, which present the same global fold, interact with two different classes of K+ channels by two different parts, of the motif.
About this Structure
2CRD is a Single protein structure of sequence from Leiurus quinquestriatus hebraeus. The following page contains interesting information on the relation of 2CRD with [Potassium Channels]. Full crystallographic information is available from OCA.
Reference
Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications., Bontems F, Gilquin B, Roumestand C, Menez A, Toma F, Biochemistry. 1992 Sep 1;31(34):7756-64. PMID:1380828
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