2KR3
Solution structure of SHA-D
Summary for 2KR3
| Entry DOI | 10.2210/pdb2kr3/pdb |
| Related | 2rmo |
| Descriptor | Spectrin alpha chain, brain (1 entity in total) |
| Functional Keywords | alpha spectrin sh3 domain, bergerac, actin capping, actin-binding, cytoskeleton, signaling protein |
| Biological source | Gallus gallus (Chicken) |
| Cellular location | Cytoplasm, cytoskeleton: P07751 |
| Total number of polymer chains | 1 |
| Total formula weight | 8124.26 |
| Authors | Khristoforov, V.S.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Gushchina, L.V.,Filimonov, V.V.,Kutyshenko, V.P. (deposition date: 2009-12-03, release date: 2010-09-15, Last modification date: 2024-05-01) |
| Primary citation | Khristoforov, V.S.,Prokhorov, D.A.,Timchenko, M.A.,Kudrevatykh, Y.A.,Gushchina, L.V.,Filimonov, V.V.,Kutyshenko, V.P. Chimeric SHA-D domain "SH3-Bergerac": 3D structure and dynamics studies Russ.J.Bioorganic Chem., 36:468-476, 2010 Cited by PubMed Abstract: Protein SHA-D of "SH3-Bergerac" chimeric proteins family was constructed by substitution of beta-turn N47-D48 in spectrin SH3-domain by KATANDKTYE amino acid sequence. Structural and dynamics properties of SHA-D in solution were studied by with the help of high-resolution NMR. The extension of SHA-D polypeptide chain in comparison with wild type of protein WT-SH3 (~ 17%) practically doesn't affect almost the total molecule topology. 3D-structure of SHA-D is practically identical to the proteins of "SH3-Bergerac" family. However there are some differences in dynamic characteristics in the region of substitution. The G52D substitution in SHA-D protein results in a destabilization of the region insertion where the conditions for conformational exchange appear. Destabilization further affects the entire SHA- D molecule making its structure more labile. PubMed: 20823919DOI: 10.1134/S1068162010040059 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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