2OAW
Structure of SHH variant of "Bergerac" chimera of spectrin SH3
Summary for 2OAW
| Entry DOI | 10.2210/pdb2oaw/pdb |
| Related | 1BK2 1SHG |
| Descriptor | Spectrin alpha chain, brain, CHLORIDE ION (3 entities in total) |
| Functional Keywords | sh3 domain, chimera, structural protein |
| Biological source | Gallus gallus (chicken) |
| Cellular location | Cytoplasm, cytoskeleton: P07751 |
| Total number of polymer chains | 4 |
| Total formula weight | 30730.28 |
| Authors | Gabdoulkhakov, A.G.,Gushchina, L.V.,Nikulin, A.D.,Nikonov, S.V.,Viguera, A.R.,Serrano, L.,Filimonov, V.V. (deposition date: 2006-12-18, release date: 2008-04-08, Last modification date: 2023-08-30) |
| Primary citation | Gushchina, L.V.,Gabdulkhakov, A.G.,Nikonov, S.V.,Mateo, P.L.,Filimonov, V.V. Structural and thermodynamic studies of Bergerac-SH3 chimeras. Biophys.Chem., 139:106-115, 2009 Cited by PubMed Abstract: Bergerac-type chimeras of spectrin SH3 were designed by extending a beta-hairpin by eight amino acids so that the extension protruded from the domain body like a "nose" being exposed to the solvent. A calorimetric study of several Bergerac-SH3 variants was carried out over a wide range of pH values and protein concentrations and the three-dimensional structure of one of them, SHH, was determined. X-ray studies confirmed that the nose had a well defined beta-structure whilst the chimera formed a stable tetramer within the crystal unit because of four tightly packed noses. In the pH range of 4-7 the heat-induced unfolding of some chimeras was complex and concentration dependent, whilst at pH values below 3.5, low protein concentrations of all the chimeras studied, including SHH, seemed to obey a monomolecular two-state unfolding model. The best set of data was obtained for the SHA variant, the unfolding heat effects of which were systematically higher than those of the WT protein (about 16.4 kJ/mol at 323 K), which may be close to the upper limit of the enthalpy gain due to 10 residue beta-hairpin folding. At the same time, the chimeras with high nose stability, which, like SHH, have a hydrophobic (IVY) cluster on their surface, showed a lower apparent unfolding heat effect, much closer to that of the WT protein. The possible reasons for this difference are discussed. PubMed: 19042078DOI: 10.1016/j.bpc.2008.10.011 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.9 Å) |
Structure validation
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