1tuc
From Proteopedia
| Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tuc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tuc OCA], [http://www.ebi.ac.uk/pdbsum/1tuc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tuc RCSB]</span> | ||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: sh3 domain]] | [[Category: sh3 domain]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:01:11 2008'' |
Revision as of 21:01, 30 March 2008
| |||||||
| , resolution 2.02Å | |||||||
|---|---|---|---|---|---|---|---|
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
ALPHA-SPECTRIN SRC HOMOLOGY 3 DOMAIN, CIRCULAR PERMUTANT, CUT AT S19-P20
Overview
We have analyzed the structure, stability and folding kinetics of circularly permuted forms of alpha-spectrin SH3 domain. All the possible permutations involving the disruption of the covalent linkage between two beta-strands forming a beta-hairpin have been done. The different proteins constructed here fold to a native conformation similar to that of wild-type protein, as demonstrated by nuclear magnetic resonance and circular dichroism. Although all the mutants have similar stabilities (they are 1 to 2 kcal mol-1 less stable than the wild-type) their rate constants for folding and unfolding are quite different. Protein engineering, in combination with kinetics indicates that the folding pathway has been changed in the circularly permuted proteins. We conclude that neither the order of secondary structure elements, nor the preservation of any of the beta-hairpins present in this domain, is crucial for the ability of the polypeptide to fold, but they influence the folding and unfolding kinetics and could determine its folding pathway.
About this Structure
1TUC is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
The order of secondary structure elements does not determine the structure of a protein but does affect its folding kinetics., Viguera AR, Blanco FJ, Serrano L, J Mol Biol. 1995 Apr 7;247(4):670-81. PMID:7723022
Page seeded by OCA on Mon Mar 31 00:01:11 2008
