1z9m
From Proteopedia
(New page: 200px<br /> <applet load="1z9m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z9m, resolution 2.4Å" /> '''Crystal Structure of...) |
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| - | [[Image:1z9m.gif|left|200px]]<br /> | + | [[Image:1z9m.gif|left|200px]]<br /><applet load="1z9m" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1z9m" size=" | + | |
caption="1z9m, resolution 2.4Å" /> | caption="1z9m, resolution 2.4Å" /> | ||
'''Crystal Structure of Nectin-like molecule-1 protein Domain 1'''<br /> | '''Crystal Structure of Nectin-like molecule-1 protein Domain 1'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Nectins are Ca(2+)-independent immunoglobulin (Ig) superfamily proteins | + | 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== | ==About this Structure== | ||
| - | 1Z9M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1Z9M is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z9M OCA]. |
==Reference== | ==Reference== | ||
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[[Category: v domain]] | [[Category: v domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:27 2008'' |
Revision as of 14:13, 21 February 2008
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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 Thu Feb 21 16:13:27 2008
Categories: Homo sapiens | Single protein | Chen, T. | Dong, X. | Gao, J. | Gong, Y. | Lin, P. | Peng, X. | Peng, Y. | Qiang, B. | Rao, Z. | Xu, F. | Yuan, J. | Ig-like domain | Nectin-like | V domain
