1dlz

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(New page: 200px<br /><applet load="1dlz" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dlz" /> '''SOLUTION STRUCTURE OF THE CHANNEL-FORMER ZER...)
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Revision as of 01:10, 25 November 2007

Image:1dlz.jpg

1dlz

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SOLUTION STRUCTURE OF THE CHANNEL-FORMER ZERVAMICIN IIB (PEPTAIBOL ANTIBIOTIC)

Overview

Spatial structure of the membrane channel-forming hexadecapeptide, zervamicin IIB, was studied by NMR spectroscopy in mixed solvents of, different polarity ranging from CDCl3/CD3OH (9:1, v/v) to CD3OH/H2O (1:1, v/v). The results show that in all solvents used the peptide has a very, similar structure that is a bent amphiphilic helix with a mean backbone, root mean square deviation (rmsd) value of ca. 0.3 A. Side chains of Trp1, Ile2, Gln3, Ile5 and Thr6 are mobile. The results are discussed in, relation to the validity of the obtained structure to serve as a building, block of zervamicin IIB ion channels.

About this Structure

1DLZ is a Protein complex structure of sequences from Emericellopsis salmosynnemata with ACE as ligand. Full crystallographic information is available from OCA.

Reference

NMR structure of the channel-former zervamicin IIB in isotropic solvents., Balashova TA, Shenkarev ZO, Tagaev AA, Ovchinnikova TV, Raap J, Arseniev AS, FEBS Lett. 2000 Jan 28;466(2-3):333-6. PMID:10682854

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