1z9m

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[[Image:1z9m.gif|left|200px]]
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{{Structure
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The line below this paragraph, containing "STRUCTURE_1z9m", creates the "Structure Box" on the page.
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{{STRUCTURE_1z9m| PDB=1z9m | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1z9m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1z9m OCA], [http://www.ebi.ac.uk/pdbsum/1z9m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1z9m RCSB]</span>
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'''Crystal Structure of Nectin-like molecule-1 protein Domain 1'''
'''Crystal Structure of Nectin-like molecule-1 protein Domain 1'''
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[[Category: Xu, F.]]
[[Category: Xu, F.]]
[[Category: Yuan, J.]]
[[Category: Yuan, J.]]
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[[Category: ig-like domain]]
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[[Category: Ig-like domain]]
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[[Category: nectin-like]]
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[[Category: Nectin-like]]
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[[Category: v domain]]
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[[Category: V domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:21:19 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:32:38 2008''
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Revision as of 14:21, 3 May 2008

Image:1z9m.gif

Template:STRUCTURE 1z9m

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 Page seeded by OCA on Sat May 3 17:21:19 2008

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