1E6H

A-SPECTRIN SH3 DOMAIN A11V, M25I, V44I, V58L MUTANTS

Summary for 1E6H

• Entry DOI: 10.2210/pdb1e6h/pdb
• Related: 1AEY 1AJ3 1BK2 1CUN 1E6G 1SHG 1TUC 1TUD
• Descriptor: SPECTRIN ALPHA CHAIN (2 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: 7267.31

Authors

Vega, M.C.,Serrano, L. (deposition date: 2000-08-17, release date: 2002-05-23, Last modification date: 2023-12-13)

Primary citation

Ventura, S.,Vega, M.C.,Lacroix, E.,Angrand, I.,Spagnolo, L.,Serrano, L.
Conformational Strain in the Hydrophobic Core and its Implications for Protein Folding and Design
Nat.Struct.Biol., 9:485-, 2002

PubMed Abstract: We have designed de novo 13 divergent spectrin SH3 core sequences to determine their folding properties. Kinetic analysis of the variants with stability similar to that of the wild type protein shows accelerated unfolding and refolding rates compatible with a preferential stabilization of the transition state. This is most likely caused by conformational strain in the native state, as deletion of a methyl group (Ile-->Val) leads to deceleration in unfolding and increased stability (up to 2 kcal x mol(-1)). Several of these Ile-->Val mutants have negative phi(-U) values, indicating that some noncanonical phi(-U) values might result from conformational strain. Thus, producing a stable protein does not necessarily mean that the design process has been entirely successful. Strained interactions could have been introduced, and a reduction in the buried volume could result in a large increase in stability and a reduction in unfolding rates.

PubMed: 12006985
DOI: 10.1038/NSB799

Experimental method

X-RAY DIFFRACTION (2.01 Å)