1DRO
NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN
Summary for 1DRO
| Entry DOI | 10.2210/pdb1dro/pdb |
| Descriptor | BETA-SPECTRIN (1 entity in total) |
| Functional Keywords | cytoskeleton |
| Biological source | Drosophila melanogaster (fruit fly) |
| Total number of polymer chains | 1 |
| Total formula weight | 13583.06 |
| Authors | Zhang, P.,Talluri, S.,Deng, H.,Branton, D.,Wagner, G. (deposition date: 1995-09-29, release date: 1996-04-03, Last modification date: 2024-05-22) |
| Primary citation | Zhang, P.,Talluri, S.,Deng, H.,Branton, D.,Wagner, G. Solution structure of the pleckstrin homology domain of Drosophila beta-spectrin. Structure, 3:1185-1195, 1995 Cited by PubMed Abstract: The pleckstrin homology (PH) domain, which is approximately 100 amino acids long, has been found in about 70 proteins involved in signal transduction and cytoskeletal function, a frequency comparable to SH2 (src homology 2) and SH3 domains. PH domains have been shown to bind the beta gamma-subunits of G-proteins and phosphatidylinositol 4,5-bisphosphate (PIP2). It is conceivable that the PH domain of beta-spectrin plays a part in the association of spectrin with the plasma membrane of cells. PubMed: 8591029DOI: 10.1016/S0969-2126(01)00254-4 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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