CGC Bibliography Paper 5472

Coordinated folding and association of the LIN-2, -7 (L27) domain.

Harris BZ, Venkatasubrahmanyan S, Lim WA

Medline:

12110687

Citation:

Journal of Biological Chemistry 277: 34902-34908 2002

Type:

ARTICLE

Genes:

glr-1 let-23 lin-2 lin-7 lin-10

Abstract:

(L) under bar IN-(2) under bar, -(7) under bar (L27) homology domains are putative protein-protein interaction modules found in several scaffold proteins involved in the assembly of polarized cell-signaling structures. These specific interaction pairs are well conserved across metazoan species, from worms to man. We have expressed and purified L27 domains from multiple species and find that certain domains from proteins such as Caenorhabditis elegans LIN-2 and LIN-7 can specifically heterodimerize. Biophysical analysis of interacting L27 domains demonstrates that the domains interact with a 1:1 stoichiometry. Circular dichroism studies reveal that the domains appear to function as an obligate heterodimer; individually the domains are largely unfolded, but when associated they show a significant increase in helicity, as well as a cooperative unfolding transition. These novel obligate interacting pairs are likely to play a key role in regulating the organization of signaling proteins at