1UUE

a-SPECTRIN SH3 DOMAIN (V44T, D48G MUTANT)

Summary for 1UUE

• Entry DOI: 10.2210/pdb1uue/pdb
• Related: 1AEY 1AJ3 1BK2 1CUN 1E6G 1E6H 1E7O 1G2B 1H8K 1HD3 1M8M 1NEG 1PWT 1QKW 1QKX 1SHG 1TUC 1TUD
• Descriptor: SPECTRIN ALPHA CHAIN (2 entities in total)
• Functional Keywords: sh3-domain, sh3, spectrin, cytoskeleton, membrane, calmodulin-binding, actin-binding, calcium-binding
• Biological source: GALLUS GALLUS (CHICKEN)
• Total number of polymer chains: 1
• Total formula weight: 7173.18

Authors

Vega, M.C.,Fernandez, A.,Wilmanns, M.,Serrano, L. (deposition date: 2003-12-18, release date: 2004-02-19, Last modification date: 2023-12-13)

Primary citation

Fernandez, A.,Vega, M.C.,Wilmanns, M.,Serrano, L.
Solvation in Protein Folding Analysis: Combination of Theoretical and Experimental Approaches
Proc.Natl.Acad.Sci.USA, 101:2834-, 2004

PubMed Abstract: An effort to combine theoretical analyses and protein engineering methods has been made to probe the folding mechanism of SH3 by using Energy Landscape Theory and a phi-value analysis. Particular emphasis was given to core residues and the effect of desolvation during the folding event by replacing the core valines with isosteric threonines. These mutations have the advantage of keeping the core structurally invariant while affecting core stability relative to the unfolded state. Although the valines that form the core appear spatially invariant, the folding kinetics of their threonine mutants varies, indicating their different extent of solvation in the transition-state ensemble. Theoretical studies predicted the distribution of folding kinetics of threonine mutants without previous knowledge of the measured rates. This initial success encourages further investigations of the molecular details behind these macroscopic phenomena and of the role of solvation in the folding mechanism.

PubMed: 14978284
DOI: 10.1073/PNAS.0304180101

Experimental method

X-RAY DIFFRACTION (2.6 Å)