title: How does conformational flexibility influence key structural features involved in activation of anaplastic lymphoma kinase?
abstract: Anaplastic Lymphoma Kinase (ALK) plays a major role in developing tumor processes and therefore has emerged as a validated therapeutic target. Applying atomistic molecular dynamics simulations on the wild type enzyme and the nine most frequently occurring and clinically important activation mutants we revealed important conformational effects on key interactions responsible for the activation of the enzyme.
authors.affiliation: Department of Applied Sciences, Faculty of Health and Life Sciences, Northumbria University, Newcastle upon Tyne, NE1 8ST, UK. christo.christov@northumbria.ac.uk tatyana.karabencheva-christova@northumbria.ac.uk.
authors.forename: Tatyana G
authors.initials: TG
authors.lastname: Karabencheva
authors.forename: Christian C
authors.initials: CC
authors.lastname: Lee
authors.forename: Gary W
authors.initials: GW
authors.lastname: Black
authors.forename: Rossen
authors.initials: R
authors.lastname: Donev
authors.forename: Christo Z
authors.initials: CZ
authors.lastname: Christov
mesh_terms: D000077548:Anaplastic Lymphoma Kinase; D020134:Catalytic Domain; D019295:Computational Biology; D018360:Crystallography, X-Ray; D006801:Humans; D056004:Molecular Dynamics Simulation; D009154:Mutation; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D020794:Receptor Protein-Tyrosine Kinases / Q000737:chemistry* / Q000235:genetics
chemical_list: C000626173:ALK protein, human; D000077548:Anaplastic Lymphoma Kinase; D020794:Receptor Protein-Tyrosine Kinases