1Z9M

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

Summary for 1Z9M

• Entry DOI: 10.2210/pdb1z9m/pdb
• Descriptor: GAPA225 (2 entities in total)
• Functional Keywords: nectin-like, ig-like domain, v domain, cell adhesion
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 2
• Total formula weight: 31737.30

Authors

Dong, X.,Xu, F.,Gong, Y.,Gao, J.,Lin, P.,Chen, T.,Peng, Y.,Qiang, B.,Yuan, J.,Peng, X.,Rao, Z. (deposition date: 2005-04-03, release date: 2006-02-07, Last modification date: 2024-10-16)

Primary citation

Dong, X.,Xu, F.,Gong, Y.,Gao, J.,Lin, P.,Chen, T.,Peng, Y.,Qiang, B.,Yuan, J.,Peng, X.,Rao, Z.
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
J.Biol.Chem., 281:10610-10617, 2006

PubMed Abstract: 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.

PubMed: 16467305
DOI: 10.1074/jbc.M513459200

Experimental method

X-RAY DIFFRACTION (2.4 Å)