1j0t
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(New page: 200px<br /><applet load="1j0t" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j0t" /> '''The solution structure of molt-inhibiting ho...)
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Revision as of 15:43, 20 November 2007
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The solution structure of molt-inhibiting hormone from the kuruma prawn
Overview
Molting in crustaceans is controlled by molt-inhibiting hormone (MIH) and, ecdysteroids. It is presumed that MIH inhibits the synthesis and the, secretion of ecdysteroids by the Y-organ, resulting in molt suppression., The amino acid sequence of MIH is similar to that of crustacean, hyperglycemic hormone (CHH), and therefore, they form a peptide family, referred to as the CHH family. Most of the CHH family peptides show no, cross-activity, whereas a few peptides show multiple hormonal activities., To reveal the structural basis of this functional specificity, we, determined the solution structure of MIH from the Kuruma prawn, Marsupenaeus japonicus and compared the solution structure of MIH with a, homology-modeled structure of M. japonicus CHH. The solution structure of, MIH consisted of five alpha-helices and no beta-structures, constituting a, novel structural motif. The homology-modeled structure of M. japonicus CHH, was very similar to the solution structure of MIH with the exception of, the absence of the N-terminal alpha-helix and the C-terminal tail, which, were sterically close to each other. The surface properties of MIH around, this region were quite different from those of CHH. These results strongly, suggest that this region is a functionally important site for conferring, molt-inhibiting activity.
About this Structure
1J0T is a Single protein structure of sequence from Marsupenaeus japonicus. Full crystallographic information is available from OCA.
Reference
The solution structure of molt-inhibiting hormone from the Kuruma prawn Marsupenaeus japonicus., Katayama H, Nagata K, Ohira T, Yumoto F, Tanokura M, Nagasawa H, J Biol Chem. 2003 Mar 14;278(11):9620-3. Epub 2003 Jan 7. PMID:12519766
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