3d12

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===Crystal Structures of Nipah Virus G Attachment Glycoprotein in Complex with its Receptor Ephrin-B3===
===Crystal Structures of Nipah Virus G Attachment Glycoprotein in Complex with its Receptor Ephrin-B3===
{{ABSTRACT_PUBMED_18632560}}
{{ABSTRACT_PUBMED_18632560}}
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==Function==
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[[http://www.uniprot.org/uniprot/GLYCP_NIPAV GLYCP_NIPAV]] Interacts with host ephrinB2/EFNB2 or ephrin B3/EFNB3 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.<ref>PMID:17470910</ref> <ref>PMID:15961384</ref> [[http://www.uniprot.org/uniprot/EFNB3_MOUSE EFNB3_MOUSE]] Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons.<ref>PMID:10704386</ref>
==About this Structure==
==About this Structure==
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[[3d12]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Nipah_virus Nipah virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D12 OCA].
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[[3d12]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice] and [http://en.wikipedia.org/wiki/Nipav Nipav]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3D12 OCA].
==See Also==
==See Also==
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==Reference==
==Reference==
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<ref group="xtra">PMID:018632560</ref><references group="xtra"/>
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<ref group="xtra">PMID:018632560</ref><references group="xtra"/><references/>
[[Category: Exo-alpha-sialidase]]
[[Category: Exo-alpha-sialidase]]
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[[Category: Mus musculus]]
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[[Category: Lk3 transgenic mice]]
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[[Category: Nipah virus]]
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[[Category: Nipav]]
[[Category: Broder, C C.]]
[[Category: Broder, C C.]]
[[Category: Chan, Y P.]]
[[Category: Chan, Y P.]]

Revision as of 04:23, 13 February 2014

Template:STRUCTURE 3d12

Contents

Crystal Structures of Nipah Virus G Attachment Glycoprotein in Complex with its Receptor Ephrin-B3

Template:ABSTRACT PUBMED 18632560

Function

[GLYCP_NIPAV] Interacts with host ephrinB2/EFNB2 or ephrin B3/EFNB3 to provide virion attachment to target cell. This attachment induces virion internalization predominantly through clathrin-mediated endocytosis.[1] [2] [EFNB3_MOUSE] Cell surface transmembrane ligand for Eph receptors, a family of receptor tyrosine kinases which are crucial for migration, repulsion and adhesion during neuronal, vascular and epithelial development. Binds promiscuously Eph receptors residing on adjacent cells, leading to contact-dependent bidirectional signaling into neighboring cells. The signaling pathway downstream of the receptor is referred to as forward signaling while the signaling pathway downstream of the ephrin ligand is referred to as reverse signaling. May play a pivotal role in forebrain function. Binds to, and induce the collapse of, commissural axons/growth cones in vitro. May play a role in constraining the orientation of longitudinally projecting axons.[3]

About this Structure

3d12 is a 4 chain structure with sequence from Lk3 transgenic mice and Nipav. Full crystallographic information is available from OCA.

See Also

Reference

  • Xu K, Rajashankar KR, Chan YP, Himanen JP, Broder CC, Nikolov DB. Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proc Natl Acad Sci U S A. 2008 Jul 22;105(29):9953-8. Epub 2008 Jul 16. PMID:18632560
  1. ↑ Diederich S, Maisner A. Molecular characteristics of the Nipah virus glycoproteins. Ann N Y Acad Sci. 2007 Apr;1102:39-50. PMID:17470910 doi:http://dx.doi.org/10.1196/annals.1408.003
  2. ↑ Diederich S, Moll M, Klenk HD, Maisner A. The nipah virus fusion protein is cleaved within the endosomal compartment. J Biol Chem. 2005 Aug 19;280(33):29899-903. Epub 2005 Jun 16. PMID:15961384 doi:http://dx.doi.org/10.1074/jbc.M504598200
  3. ↑ Imondi R, Wideman C, Kaprielian Z. Complementary expression of transmembrane ephrins and their receptors in the mouse spinal cord: a possible role in constraining the orientation of longitudinally projecting axons. Development. 2000 Apr;127(7):1397-410. PMID:10704386

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