L27 Heterodimer From C. Elegans Lin-7 and H. Sapiens Lin-2 Scaffold Proteins
L27 Heterodimer From Lin-7 and Lin-2 Scaffold Proteins

assembly of synaptic signaling complexes

NMR assignment of the L27 heterodimer from LIN-2 and LIN-7 scaffold proteins.

Anticipated publication in the December issue of JBC.
A general model for preferential hetero-oligomerization of LIN-2/7 domains: mechanism underlying directed assembly of supramolecular signaling complexes.

NMR Structure Of L27 Heterodimer From C. Elegans Lin-7 and H. Sapiens Lin-2 Scaffold Proteins

N-terminal oligoHis tag followed by TEV cleavage site, L27 domain from LIN-7, Gly Ser linker repeat, and L27 domain from LIN-2C

Met1-Ser23 1 "purification tag"
Leu24-Ala89 2 "dimerization unit"
Gly90-Ser97 3 linker
Asn98-Pro164 4 "dimerization unit"

L27 domains from Lin-7 and Lin-2C were expressed as a linked construct to ensure
a 1:1 ratio and to improve solubility,

NMR Assignments of L27 Heterodimer From C. Elegans Lin-7 and H. Sapiens Lin-2
Scaffold Proteins

20mM HEPES, pH 8.0, with 0.5 mM Tris(2-carboxyethyl) phophine hydrochloride (TCEP)