Structural basis for ligand reception by anaplastic lymphoma kinase.

ABSTRACT: The proto-oncogene ALK encodes anaplastic lymphoma kinase, a receptor tyrosine kinase that is expressed primarily in the developing nervous system. After development, ALK activity is associated with learning and memory¹ and controls energy expenditure, and inhibition of ALK can prevent diet-induced obesity². Aberrant ALK signalling causes numerous cancers³. In particular, full-length ALK is an important driver in paediatric neuroblastoma^4,5, in which it is either mutated⁶ or activated by ligand⁷. Here we report crystal structures of the extracellular glycine-rich domain (GRD) of ALK, which regulates receptor activity by binding to activating peptides^8,9. Fusing the ALK GRD to its ligand enabled us to capture a dim

SUBMITTER: Li T 

PROVIDER: S-EPMC8639777 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature