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Prediction of NO Oxidizable Cysteines. Larry Grant Dr. Jamil Momand Cal State L.A. Redox-based protein regulation. similar to phosphorylation. reversible detectable Plays a major role in many physiological processes. inflammation, cell channel signaling, protease activity.
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Prediction of NO Oxidizable Cysteines Larry Grant Dr. Jamil Momand Cal State L.A.
Redox-based protein regulation. similar to phosphorylation. reversible detectable Plays a major role in many physiological processes. inflammation, cell channel signaling, protease activity S-nitrosylation
COPP Project • Cysteine Oxidation Prediction Program • Will be web-based • Capable of predicting cysteine reactivity based on primary sequence and/or structure data. • 4 kinds of reactivity
My Project • Generate parameters based on sequence information to predict NO susceptibility. • Stamler et, al have proposed a short motiff based on 27 sequences. • (Lys,Arg,His,Asp,Glu) – Cys – (Asp/Glu)
Extracting parameters… • Data Mining • Target of 100-150 oxidizable thiols • 71 s-nitrosylated Cys from 63 different proteins. -20………-10…………..-1C+1….…+10……...…+20
PSIPRED Analyzer • Three major functions: • Average confidence • Secondary structure frequency • Residue frequency
H H H H C C C C C C 6 6 6 6 6 6 6 6 6 6 Green = Polar Blue = Basic Black = Hydrophobic Red = Acidic
The future • Support Vector Machines • relative solvent accessibility • minimum of 1.3 Å2 • hydrophobicity, acidity, side-chain length
References • Stamler, et al. “(S)NO signals: translocation, regulation, and a consensus motif.”Neuron. 1997 May;18(5):691-6. • Sanchez, et al. “Prediction of reversibly oxidized protein cysteine thiols using protein structure properties.” Protein Sci. 2008 Mar;17(3):473-81. • Hess, et al. “Protein S-nitrosylation - Purview and Parameters.” Nat Rev Mol Cell Biol. 2005 Feb;6(2):150-66.
Thank you for all of your help: Dr. Momand Dr. Sharp Dr. Warter-Perez Dr. Johnston Ronnie Cheng My fellow interns. Funded by: Acknowledgements