Identification of Secondary Structure of Extracellular Signal Regulated Kinase (ERK) Interacting Proteins and Their Domain: An in Silico Study
Identification of Secondary Structure of Extracellular Signal Regulated Kinase (ERK) Interacting Proteins and Their Domain: An in Silico Study作者机构：Cellular and Molecular Neurobiology & Drug Targeting Laboratory Department of Zoology Indira Gandhi National Tribal University Amarkantak (MP) (MP)-484 887 India
出 版 物：《World Journal of Neuroscience》 (神经科学国际期刊（英文）)
年 卷 期：2021年第11卷第1期
页 面：67-89页
主 题：ERK Secondary Structure Motif Scan Random Coils Alpha Helix Protein Kinases
摘 要：ERK is involved in multiple cell signaling pathways through its interacting proteins. By in silico analysis, earlier we have identified 22 putative ERK interacting proteins namely;ephrin type-B receptor 2 isoform 2 precursor (EPHB2), mitogen-activated protein kinase 1(MAPK1), interleukin-17 receptor D precursor (IL17RD), WD repeat domain containing 83 (WDR83), tescalcin (Tesc), mitogen-activated protein kinase kinase kinase 4 (MAPP3K4), kinase suppressor of Ras2 (KSR2), mitogen-activated protein kinase kinase 6 (MAP3K6), UL16 binding protein 2 (ULBP2), UL16 binding protein 1 (ULBP1), dual specificity phosphatase 14 (DUSP14), dual specificity phosphatase 6 (DUSP6), hyaluronan-mediated motility receptor (RHAMM), kinase D interacting substrate of 220kDa (KININS220), membrane-associated guanylate kinase (MAGI3), phosphoprotein enriched in astrocytes 15(PEA15), typtophenyl-tRNA synthetase, cytoplasmic (WARS), dual specificity phosphatase 9 (DUSP9), mitogen-activated protein kinase kinase kinase 1(MAP3K1), UL16 binding protein 3 (ULBP3), SLAM family member 7 isoform a precursor (SLAMMF7) and mitogen activated protein kinase kinase kinase 11 (MAP3K11) (Table 1). However, prediction of secondary structure and domain/motif present in aforementioned ERK interacting proteins is not studied. In this paper, insilico prediction of secondary structure of ERK interacting proteins was done by SOPMA and motif/domain identification using motif search. Briefly, SOPMA predicted higher random coil and alpha helix percentage in these proteins (Table 2) and motif scan predicted serine/threonine kinases active site signature and protein kinase ATP binding region in majority of ERK interacting proteins. Moreover, few have commonly dual specificity protein phosphatase family and tyrosine specific protein phosphatase domains (Table 3). Such study may be helpful to design engineered molecules for regulating ERK dependent pathways in disease condition.
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