Structural Plasticity of Neurexin 1α: Implications for its Role as Synaptic Organizer.

ABSTRACT: α-Neurexins are synaptic organizing molecules implicated in neuropsychiatric disorders. They bind and arrange an array of different partners in the synaptic cleft. The extracellular region of neurexin 1α (n1α) contains six LNS domains (L1-L6) interspersed by three Egf-like repeats. N1α must encode highly evolved structure-function relationships in order to fit into the narrow confines of the synaptic cleft, and also recruit its large, membrane-bound partners. Internal molecular flexibility could provide a solution; however, it is challenging to delineate because currently no structural methods permit high-resolution structure determination of large, flexible, multi-domain protein molecules. To investigate the structural plasticity of n1α, in particular the conformation of domains that carr

SUBMITTER: Liu J 

PROVIDER: S-EPMC6223652 | biostudies-literature | 2018 Oct

REPOSITORIES: biostudies-literature