Structural prediction and in silico physicochemical characterization for mouse caltrin I and bovine caltrin proteins.

CORONEL CE; SOTTILE AE; GRASSO EJ

San Miguel de Tucumán

Congreso; Sociedad Argentina de Biofísica IIILAFeBS, IX IberoAmerican Congress of Biophysics, XLV SAB Annual Meeting; 2016

Sociedad Argentina de Biofísica

It is known that caltrin (calcium transport inhibitor) protein binds tosperm cells during ejaculation and inhibits extracellular Ca2+ uptake.Although the sequence and some biological features of mouse caltrin Iand bovine caltrin are known, their physicochemical properties and tertiarystructure are mainly unknown. We predicted the 3D structures ofmouse caltrin I and bovine caltrin by molecular homology modeling andthreading. Surface electrostatic potentials and electric fields were calculatedusing the Poisson-Boltzmann equation. Several different bioinformaticstools and available web servers were used to thoroughly analyzethe physicochemical characteristics of both proteins, such as their Kyteand Doolittle Hydropathy scores and helical wheel projections. The resultspresented in this work significantly aid further understanding ofthe molecular mechanisms of caltrin proteins modulating physiologicalprocesses associated with fertilization.