1le3
From Proteopedia
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| - | [[Image:1le3.jpg|left|200px]] | + | [[Image:1le3.jpg|left|200px]] |
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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''' | + | {{Structure |
| + | |PDB= 1le3 |SIZE=350|CAPTION= <scene name='initialview01'>1le3</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''NMR Structure of Tryptophan Zipper 4: A Stable Beta-Hairpin Peptide Based on the C-terminal Hairpin of the B1 Domain of Protein G''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LE3 is a [ | + | 1LE3 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. This structure supersedes the now removed PDB entry 1HS0. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LE3 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: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cochran, A G.]] | [[Category: Cochran, A G.]] | ||
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[[Category: type i beta-turn]] | [[Category: type i beta-turn]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:29:51 2008'' |
Revision as of 10:29, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. This structure supersedes 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 Thu Mar 20 12:29:51 2008
