In silico Sequence Analysis, Structure Prediction and Function Annotation of Human Bcl-X Beta Protein

Abstract

Bcl-X proteins are the one of the best categorized member of the Bcl-2 protein families which acts as primary regulators of apoptosis in mammalian cells. The Bcl-X proteins are potential anti-cancer drug targets. In this study, the tertiary structure of the beta isoform of the apoptosis regulator Bcl-X in humans (h-Bcl-Xβ) has been predicted by fold-recognition (threading) approach. In silico assessment of the h-Bcl-Xβ protein revealed the characteristic structural features of anti-apoptotic Bcl-2 protein family in h-Bcl-Xβ protein. The predicted model was comprised of BH1-BH4 domains, seven alpha-helices and a C-terminal transmembrane domain for membrane localization and sub-cellular targeting. Quality assessment of the predict model confirmed its reliability as fairly good model. Active sites of h-Bcl-Xβ protein were identified using CASTp server. The future work can be directed towards drug designing for cancer treatment by regulating the activity of h-Bcl-Xβ proteins.

Keywords

• h-Bcl-Xβ
• Threading
• Apoptosis
• Cancer