Targeting cysteine rich C1 domain of Scaffold protein Kinase Suppressor of Ras (KSR) with anthocyanidins and flavonoids – a binding affinity characterization study

BACK TO CONTENTS | PDF | PREVIOUS | NEXT

Title	Targeting cysteine rich C1 domain of Scaffold protein Kinase Suppressor of Ras (KSR) with anthocyanidins and flavonoids – a binding affinity characterization study
Authors	Dhananjayan Karthik¹*, Pulak Majumder², Sivanandy Palanisamy³, Kalathil Khairunnisa⁴ & Varsha Venugopal⁵
Affiliation	¹Department of Pharmacology, Amrita School of Pharmacy, AIMS Health Science Campus, Amrita Vishwa Vidyapeetham University, Kochi, Kerala, India; ²Department of Pharmacognosy, Acharya & B.M.Reddy College of Pharmacy, Bangalore, Karnataka, India; ³Department of Pharmacy Practice, International Medical University, Kualalampur, Malaysia; ⁴Department of Pharmacology, Grace College of Pharmacy, Palakkad, Kerala, India; ⁵Department of Pharmacognosy, Government Medical College, Thiruvananthapuram, Kerala, India
Email	karthikdcology@gmail.com; *Corresponding author
Article Type	Hypothesis
Date	Received September 05, 2014; Accepted September 06, 2014; Published September 30, 2014
Abstract	Kinase Suppressor of Ras (KSR) is a molecular scaffold that interacts with the core kinase components of the ERK cascade, Raf, MEK, ERK to provide spatial and temporal regulation of Ras-dependent ERK cascade signaling. Interruption of this mechanism can have a high influence in inhibiting the downstream signaling of the mutated tyrosine kinase receptor kinase upon ligand binding. Still none of the studies targeted to prevent the binding of Raf, MEK binding on kinase suppressor of RAS. In that perspective the cysteine rich C1 domain of scaffold proteins kinase suppressor of Ras-1 was targeted rather than its ATP binding site with small ligand molecules like flavones and anthocyanidins and analyzed through insilico docking studies. The binding energy evaluation shows the importance of hydroxyl groups at various positions on the flavone and anthocyanidin nucleus. Over all binding interaction shows these ligands occupied the potential sites of cysteine rich C1 domain of scaffold protein KSR.
Keywords	Kinase suppressor of Ras, MAPK signaling, flavones, anthocyanidins, insilico docking, AutoDock 4.2.6, Neoplasia
Citation	Karthik et al. Bioinformation 10(9): 580-585 (2014)
Edited by	P Kangueane
ISSN	0973-2063
Publisher	Biomedical Informatics
License	This is an Open Access article which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. This is distributed under the terms of the Creative Commons Attribution License.