2cdt

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{{STRUCTURE_2cdt| PDB=2cdt | SCENE= }}
{{STRUCTURE_2cdt| PDB=2cdt | SCENE= }}
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'''ALPHA-SPECTRIN SH3 DOMAIN A56S MUTANT'''
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===ALPHA-SPECTRIN SH3 DOMAIN A56S MUTANT===
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==Overview==
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Site-directed mutagenesis has been used to produce local stability changes at two regions of the binding site surface of the alpha-spectrin SH3 domain (Spc-SH3) differing in their intrinsic stability. Mutations were made at residue 56, located at the solvent-exposed side of the short 3(10) helix, and at residue 21 in the tip of the flexible RT-loop. NMR chemical-shift analysis and X-ray crystallography indicated negligible changes produced by the mutations in the native structure limited to subtle rearrangements near the mutated residue and at flexible loops. Additionally, mutations do not alter importantly the SH3 binding site structure, although produce significant changes in its affinity for a proline-rich decapeptide. The changes in global stability measured by differential scanning calorimetry are consistent the local energy changes predicted by theoretical models, with the most significant effects observed for the Ala-Gly mutations. Propagation of the local stability changes throughout the domain structure has been studied at a per-residue level of resolution by NMR-detected amide hydrogen-deuterium exchange (HX). Stability propagation is remarkably efficient in this small domain, apparently due to its intrinsically low stability. Nevertheless, the HX-core of the domain is not fully cooperative, indicating the existence of co-operative subunits within the core, which is markedly polarized. An equilibrium phi-analysis of the changes in the apparent Gibbs energies of HX per residue produced by the mutations has allowed us to characterize structurally the conformational states leading to HX. Some of these states resemble notably the folding transition state of the Spc-SH3 domain, suggesting a great potential of this approach to explore the folding energy landscape of proteins. An energy perturbation propagates more effectively from a flexible region to the core than in the opposite direction, because the former affects a broader region of the energy landscape than the latter. This might be of importance in understanding the special thermodynamic signature of the SH3-peptide interaction and the relevance of the dual character of SH3 binding sites.
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(as it appears on PubMed at http://www.pubmed.gov), where 17330285 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17330285}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
Cooperative propagation of local stability changes from low-stability and high-stability regions in a SH3 domain., Casares S, Lopez-Mayorga O, Vega MC, Camara-Artigas A, Conejero-Lara F, Proteins. 2007 May 15;67(3):531-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17330285 17330285]
Cooperative propagation of local stability changes from low-stability and high-stability regions in a SH3 domain., Casares S, Lopez-Mayorga O, Vega MC, Camara-Artigas A, Conejero-Lara F, Proteins. 2007 May 15;67(3):531-47. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17330285 17330285]
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Crystal structure of a Src-homology 3 (SH3) domain., Musacchio A, Noble M, Pauptit R, Wierenga R, Saraste M, Nature. 1992 Oct 29;359(6398):851-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/1279434 1279434]
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Sh3-domain]]
[[Category: Sh3-domain]]
[[Category: Structural protein]]
[[Category: Structural protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 14 11:37:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:42:42 2008''

Revision as of 10:42, 29 July 2008

Image:2cdt.png

Template:STRUCTURE 2cdt

ALPHA-SPECTRIN SH3 DOMAIN A56S MUTANT

Template:ABSTRACT PUBMED 17330285

About this Structure

2CDT is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.

Reference

Cooperative propagation of local stability changes from low-stability and high-stability regions in a SH3 domain., Casares S, Lopez-Mayorga O, Vega MC, Camara-Artigas A, Conejero-Lara F, Proteins. 2007 May 15;67(3):531-47. PMID:17330285

Crystal structure of a Src-homology 3 (SH3) domain., Musacchio A, Noble M, Pauptit R, Wierenga R, Saraste M, Nature. 1992 Oct 29;359(6398):851-5. PMID:1279434

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