2MDU
Circular Permutant of the WW Domain with Loop 1 Excised
Summary for 2MDU
| Entry DOI | 10.2210/pdb2mdu/pdb |
| Related | 1pin 2kcf |
| NMR Information | BMRB: 19503 |
| Descriptor | Pin1 WW domain (1 entity in total) |
| Functional Keywords | circular permutation, miniprotein, dynamics, folding, isomerase |
| Total number of polymer chains | 1 |
| Total formula weight | 3794.39 |
| Authors | Kier, B.L. (deposition date: 2013-09-18, release date: 2014-01-15, Last modification date: 2024-05-01) |
| Primary citation | Kier, B.L.,Anderson, J.M.,Andersen, N.H. Circular Permutation of a WW Domain: Folding Still Occurs after Excising the Turn of the Folding-Nucleating Hairpin. J.Am.Chem.Soc., 136:741-749, 2014 Cited by PubMed Abstract: A hyperstable Pin1 WW domain has been circularly permuted via excision of the fold-nucleating turn; it still folds to form the native three-strand sheet and hydrophobic core features. Multiprobe folding dynamics studies of the normal and circularly permuted sequences, as well as their constituent hairpin fragments and comparable-length β-strand-loop-β-strand models, indicate 2-state folding for all topologies. N-terminal hairpin formation is the fold nucleating event for the wild-type sequence; the slower folding circular permutant has a more distributed folding transition state. PubMed: 24350581DOI: 10.1021/ja410824x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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