1ZL8

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

Summary for 1ZL8

• Entry DOI: 10.2210/pdb1zl8/pdb
• Related: 1RSO 1VF6 1Y74 1Y76
• Descriptor: LIN-7, Peripheral plasma membrane protein CASK (2 entities in total)
• Functional Keywords: heterodimer, l27, alpha helix, scaffold, assembly, specificity, signaling, protein binding
• Biological source: Caenorhabditis elegans; More
• Cellular location: Nucleus (By similarity): O14936
• Total number of polymer chains: 2
• Total formula weight: 12277.71

Authors

Petrosky, K.Y.,Ou, H.D.,Lohr, F.,Dotsch, V.,Lim, W.A. (deposition date: 2005-05-05, release date: 2005-09-13, Last modification date: 2024-05-01)

Primary citation

Petrosky, K.Y.,Ou, H.D.,Lohr, F.,Dotsch, V.,Lim, W.A.
A General Model for Preferential Hetero-oligomerization of LIN-2/7 Domains: Mechanism Underlying Directed Assembly of Supramolecular Signaling Complexes
J.Biol.Chem., 280:38528-38536, 2005

PubMed Abstract: 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.

PubMed: 16147993
DOI: 10.1074/jbc.M506536200

Experimental method

SOLUTION NMR