Profilin oligomerization and its effect on poly (l-proline) binding and phosphorylation |
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| Authors: | Radhika V. Korupolu M.S. Achary F. Aneesa K. Sathish R. Wasia M. Sairam H.A. Nagarajaram Surya S. Singh |
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| Affiliation: | aDepartment of Biochemistry, Osmania University, Hyderabad 500007, India;bCentre for DNA Fingerprinting and Diagnostics, Hyderabad, India;cDefence Institute of Physiology and Allied Sciences, DRDO, Lucknow Road, Delhi, India |
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| Abstract: | Profilin is a cytoskeletal protein that interacts specifically with actin, phosphoinositides and poly (l-proline). Experimental results and in silico studies revealed that profilin exists as dimer and tetramer. Profilin oligomers possess weak affinity to poly (l-proline) due to unavailability of binding sites in dimers and tetramers. Phosphorylation studies indicate that profilin dimers are not phosphorylated while teramers are preferentially phosphorylated over monomers. In silico studies revealed that PKC phosphorylation site, S137 is buried in dimer while it is accessible in tetramer. |
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| Keywords: | Profilin Oligomerization Phosphorylation |
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