1HD3
A-SPECTRIN SH3 DOMAIN F52Y MUTANT
Summary for 1HD3
| Entry DOI | 10.2210/pdb1hd3/pdb |
| Related | 1AEY 1AJ3 1BK2 1CUN 1E6G 1E6H 1E7O 1PWT 1QKW 1QKX 1SHG 1TUC 1TUD |
| Descriptor | SPECTRIN ALPHA CHAIN, SULFATE ION, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | sh3-domain, cytoskeleton, calmodulin-binding, actin-binding |
| Biological source | GALLUS GALLUS (CHICKEN) |
| Total number of polymer chains | 1 |
| Total formula weight | 7525.49 |
| Authors | Vega, M.C.,Viguera, A.R.,Serrano, L. (deposition date: 2000-11-06, release date: 2001-11-01, Last modification date: 2023-12-13) |
| Primary citation | Viguera, A.R.,Vega, C.,Serrano, L. Unspecific Hydrophobic Stabilization of Folding Transition States Proc.Natl.Acad.Sci.USA, 99:5349-, 2002 Cited by PubMed Abstract: Here we present a method for determining the inference of non-native conformations in the folding of a small domain, alpha-spectrin Src homology 3 domain. This method relies on the preservation of all native interactions after Tyr/Phe exchanges in solvent-exposed, contact-free positions. Minor changes in solvent exposure and free energy of the denatured ensemble are in agreement with the reverse hydrophobic effect, as the Tyr/Phe mutations slightly change the polypeptide hydrophilic/hydrophobic balance. Interestingly, more important Gibbs energy variations are observed in the transition state ensemble (TSE). Considering the small changes induced by the H/OH replacements, the observed energy variations in the TSE are rather notable, but of a magnitude that would remain undetected under regular mutations that alter the folded structure free energy. Hydrophobic residues outside of the folding nucleus contribute to the stability of the TSE in an unspecific nonlinear manner, producing a significant acceleration of both unfolding and refolding rates, with little effect on stability. These results suggest that sectors of the protein transiently reside in non-native areas of the landscape during folding, with implications in the reading of phi values from protein engineering experiments. Contrary to previous proposals, the principle that emerges is that non-native contacts, or conformations, could be beneficial in evolution and design of some fast folding proteins. PubMed: 11959988DOI: 10.1073/PNAS.072387799 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.98 Å) |
Structure validation
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