1LE1
NMR Structure of Tryptophan Zipper 2: A stable, Monomeric Beta-Hairpin with a Type I' Turn
Replaces: 1HRXSummary for 1LE1
| Entry DOI | 10.2210/pdb1le1/pdb |
| Related | 1LE0 1LE3 |
| Descriptor | Tryptophan Zipper 2 (1 entity in total) |
| Functional Keywords | beta-hairpin, type i' turn, de novo protein |
| Total number of polymer chains | 1 |
| Total formula weight | 1608.78 |
| Authors | Cochran, A.G.,Skelton, N.J.,Starovasnik, M.A. (deposition date: 2002-04-09, release date: 2002-04-24, Last modification date: 2024-10-23) |
| Primary citation | Cochran, A.G.,Skelton, N.J.,Starovasnik, M.A. Tryptophan zippers: stable, monomeric beta -hairpins. Proc.Natl.Acad.Sci.USA, 98:5578-5583, 2001 Cited by PubMed Abstract: 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. PubMed: 11331745DOI: 10.1073/pnas.091100898 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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