1zl8

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NMR structure of L27 heterodimer from C. elegans Lin-7 and H. sapiens Lin-2 scaffold proteins

Overview

LIN-2/7 (L27) domains are protein interaction modules that preferentially, hetero-oligomerize, a property critical for their function in directing, specific assembly of supramolecular signaling complexes at synapses and, other polarized cell-cell junctions. We have solved the solution structure, of the heterodimer composed of the L27 domains from LIN-2 and LIN-7., Comparison of this structure with other L27 domain structures has allowed, us to formulate a general model for why most L27 domains form an obligate, heterodimer complex. L27 domains can be divided in two types (A and B), with each heterodimer comprising an A/B pair. We have identified two, keystone positions that play a central role in discrimination. The, residues at these positions are energetically acceptable in the context of, an A/B heterodimer, but would lead to packing defects or electrostatic, repulsion in the context of A/A and B/B homodimers. As predicted by the, model, mutations of keystone residues stabilize normally strongly, disfavored homodimers. Thus, L27 domains are specifically optimized to, avoid homodimeric interactions.

About this Structure

1ZL8 is a Protein complex structure of sequences from Caenorhabditis elegans and Homo sapiens. Full crystallographic information is available from OCA.

Reference

A general model for preferential hetero-oligomerization of LIN-2/7 domains: mechanism underlying directed assembly of supramolecular signaling complexes., Petrosky KY, Ou HD, Lohr F, Dotsch V, Lim WA, J Biol Chem. 2005 Nov 18;280(46):38528-36. Epub 2005 Sep 7. PMID:16147993

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