1z9m

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spinqualitylabelsall models 1z9m, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Nectin-like molecule-1 protein Domain 1

Overview

Nectins are Ca(2+)-independent immunoglobulin (Ig) superfamily proteins, that participate in the organization of epithelial and endothelial, junctions. Nectins have three Ig-like domains in the extracellular region, and the first one is essential in cell-cell adhesion and plays a central, role in the interaction with the envelope glycoprotein D of several, viruses. Five Nectin-like molecules (Necl-1 through -5) with similar, domain structures to those of Nectins have been identified. Necl-1 is, specifically expressed in neural tissue, has Ca(2+)-independent homophilic, and heterophilic cell-cell adhesion activity, and plays an important role, in the formation of synapses, axon bundles, and myelinated axons. Here we, report the first crystal structure of its N-terminal Ig-like V domain at, 2.4 A, providing insight into trans-cellular recognition mediated by, Necl-1. The protein crystallized as a dimer, and the dimeric form was, confirmed by size-exclusion chromatography and chemical cross-linking, experiments, indicating this V domain is sufficient for homophilic, interaction. Mutagenesis work demonstrated that Phe(82) is a key residue, for the adhesion activity of Necl-1. A model for homophilic adhesion of, Necl-1 at synapses is proposed based on its structure and previous, studies.

About this Structure

1Z9M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the V domain of human Nectin-like molecule-1/Syncam3/Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like cell-cell adhesion molecule., Dong X, Xu F, Gong Y, Gao J, Lin P, Chen T, Peng Y, Qiang B, Yuan J, Peng X, Rao Z, J Biol Chem. 2006 Apr 14;281(15):10610-7. Epub 2006 Feb 7. PMID:16467305

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