1z9m: Difference between revisions

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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="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1z9m, resolution 2.4Å" />

'''Crystal Structure of Nectin-like molecule-1 protein Domain 1'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Z9M OCA].

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==

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[[Category: v domain]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Mon Nov 12 20~~:31:~~31 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:27 2008''

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@@ Line 1: / Line 1: @@
-[[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="450" color="white" frame="true" align="right" spinBox="true"
 caption="1z9m, resolution 2.4&Aring;" />
 '''Crystal Structure of Nectin-like molecule-1 protein Domain 1'''<br />
 ==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.
+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==
-Z9M 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z9M OCA].
+Z9M 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==
@@ Line 29: / Line 28: @@
 [[Category: v domain]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:31:31 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:13:27 2008''