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1DRO

NMR STRUCTURE OF THE CYTOSKELETON/SIGNAL TRANSDUCTION PROTEIN

Summary for 1DRO
Entry DOI10.2210/pdb1dro/pdb
DescriptorBETA-SPECTRIN (1 entity in total)
Functional Keywordscytoskeleton
Biological sourceDrosophila melanogaster (fruit fly)
Total number of polymer chains1
Total formula weight13583.06
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 citationZhang, 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: 8591029
DOI: 10.1016/S0969-2126(01)00254-4
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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