1le3
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(New page: 200px<br /><applet load="1le3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1le3" /> '''NMR Structure of Tryptophan Zipper 4: A Stab...)
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Revision as of 00:44, 25 November 2007
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NMR Structure of Tryptophan Zipper 4: A Stable Beta-Hairpin Peptide Based on the C-terminal Hairpin of the B1 Domain of Protein G
Overview
A structural motif, the tryptophan zipper (trpzip), greatly stabilizes the, beta-hairpin conformation in short peptides. Peptides (12 or 16 aa in, length) with four different turn sequences are monomeric and fold, cooperatively in water, as has been observed previously for some hairpin, peptides. However, the folding free energies of the trpzips exceed, substantially those of all previously reported beta-hairpins and even, those of some larger designed proteins. NMR structures of three of the, trpzip peptides reveal exceptionally well-defined beta-hairpin, conformations stabilized by cross-strand pairs of indole rings. The, trpzips are the smallest peptides to adopt an unique tertiary fold without, requiring metal binding, unusual amino acids, or disulfide crosslinks.
About this Structure
1LE3 is a Single protein structure of sequence from [1] with NH2 as ligand. This structure superseeds the now removed PDB entry 1HS0. Full crystallographic information is available from OCA.
Reference
Tryptophan zippers: stable, monomeric beta -hairpins., Cochran AG, Skelton NJ, Starovasnik MA, Proc Natl Acad Sci U S A. 2001 May 8;98(10):5578-83. Epub 2001 May 1. PMID:11331745
Page seeded by OCA on Sun Nov 25 02:51:33 2007
