1le3
From Proteopedia
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|PDB= 1le3 |SIZE=350|CAPTION= <scene name='initialview01'>1le3</scene> | |PDB= 1le3 |SIZE=350|CAPTION= <scene name='initialview01'>1le3</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=NH2:AMINO GROUP'>NH2</scene> | + | |LIGAND= <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1le0|1LE0]], [[1le1|1LE1]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1le3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1le3 OCA], [http://www.ebi.ac.uk/pdbsum/1le3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1le3 RCSB]</span> | ||
}} | }} | ||
| Line 24: | Line 27: | ||
[[Category: Skelton, N J.]] | [[Category: Skelton, N J.]] | ||
[[Category: Starovasnik, M A.]] | [[Category: Starovasnik, M A.]] | ||
| - | [[Category: NH2]] | ||
[[Category: beta-hairpin]] | [[Category: beta-hairpin]] | ||
[[Category: type i beta-turn]] | [[Category: type i beta-turn]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:01:41 2008'' |
Revision as of 19:01, 30 March 2008
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| Ligands: | |||||||
| Related: | 1LE0, 1LE1
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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
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