1le0: Difference between revisions
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'''NMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II' turn''' | {{Structure | ||
|PDB= 1le0 |SIZE=350|CAPTION= <scene name='initialview01'>1le0</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''NMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II' turn''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1LE0 is a [ | 1LE0 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/ ]. This structure supersedes the now removed PDB entry 1HRW. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE0 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11331745 11331745] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Cochran, A G.]] | [[Category: Cochran, A G.]] | ||
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[[Category: type ii' turn]] | [[Category: type ii' turn]] | ||
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Revision as of 13:29, 20 March 2008
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Coordinates: | save as pdb, mmCIF, xml |
NMR structure of Tryptophan Zipper 1: a stable, monomeric beta-hairpin with a type II' turn
OverviewOverview
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 StructureAbout this Structure
1LE0 is a Protein complex structure of sequences from [1]. This structure supersedes the now removed PDB entry 1HRW. Full crystallographic information is available from OCA.
ReferenceReference
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 Thu Mar 20 12:29:49 2008