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4ild

From Proteopedia

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m (Protected "4ild" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4ild| PDB=4ild | SCENE= }}
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===Crystal structure of truncated Bovine viral diarrhea virus 1 E2 envelope protein===
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The entry 4ild is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/POLG_BVDVN POLG_BVDVN]] Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (Probable).<ref>PMID:14963137</ref> <ref>PMID:16051874</ref> P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity).<ref>PMID:14963137</ref> <ref>PMID:16051874</ref> Uncleaved NS2-3 is required for production of infectious virus.<ref>PMID:14963137</ref> <ref>PMID:16051874</ref> NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus.<ref>PMID:14963137</ref> <ref>PMID:16051874</ref> NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase.<ref>PMID:14963137</ref> <ref>PMID:16051874</ref> NS4A is a cofactor for the NS3 protease activity (By similarity).<ref>PMID:14963137</ref> <ref>PMID:16051874</ref> RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.<ref>PMID:14963137</ref> <ref>PMID:16051874</ref>
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Authors: Modis, Y., Li, Y., Wang, J.
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==About this Structure==
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[[4ild]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovine_viral_diarrhea_virus_1-nadl Bovine viral diarrhea virus 1-nadl]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ILD OCA].
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Description: Crystal structure of truncated Bovine viral diarrhea virus 1 E2 envelope protein
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==Reference==
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<references group="xtra"/><references/>
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[[Category: Bovine viral diarrhea virus 1-nadl]]
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[[Category: Li, Y.]]
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[[Category: Modis, Y.]]
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[[Category: Wang, J.]]
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[[Category: Bvdv1]]
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[[Category: E1 envelope protein]]
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[[Category: Viral envelope protein]]
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[[Category: Viral membrane fusion]]
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[[Category: Viral protein]]
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[[Category: Viral surface membrane]]

Revision as of 22:46, 10 April 2013

Template:STRUCTURE 4ild

Contents

Crystal structure of truncated Bovine viral diarrhea virus 1 E2 envelope protein

Function

[POLG_BVDVN] Initial binding to target cell probably involves interaction of E(rns) with glycosaminoglycans. E1 and/or E2 are responsible of cell attachment with CD46 and subsequent fusion after internalization of the virion by endocytosis (Probable).[1] [2] P7 forms a leader sequence to properly orient NS2 in the membrane (By similarity).[3] [4] Uncleaved NS2-3 is required for production of infectious virus.[5] [6] NS2 protease seems to play a vital role in viral RNA replication control and in the pathogenicity of the virus.[7] [8] NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase.[9] [10] NS4A is a cofactor for the NS3 protease activity (By similarity).[11] [12] RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome.[13] [14]

About this Structure

4ild is a 2 chain structure with sequence from Bovine viral diarrhea virus 1-nadl. Full crystallographic information is available from OCA.

Reference

  1. ↑ Agapov EV, Murray CL, Frolov I, Qu L, Myers TM, Rice CM. Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus. J Virol. 2004 Mar;78(5):2414-25. PMID:14963137
  2. ↑ Lecot S, Belouzard S, Dubuisson J, Rouille Y. Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis. J Virol. 2005 Aug;79(16):10826-9. PMID:16051874 doi:10.1128/JVI.79.16.10826-10829.2005
  3. ↑ Agapov EV, Murray CL, Frolov I, Qu L, Myers TM, Rice CM. Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus. J Virol. 2004 Mar;78(5):2414-25. PMID:14963137
  4. ↑ Lecot S, Belouzard S, Dubuisson J, Rouille Y. Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis. J Virol. 2005 Aug;79(16):10826-9. PMID:16051874 doi:10.1128/JVI.79.16.10826-10829.2005
  5. ↑ Agapov EV, Murray CL, Frolov I, Qu L, Myers TM, Rice CM. Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus. J Virol. 2004 Mar;78(5):2414-25. PMID:14963137
  6. ↑ Lecot S, Belouzard S, Dubuisson J, Rouille Y. Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis. J Virol. 2005 Aug;79(16):10826-9. PMID:16051874 doi:10.1128/JVI.79.16.10826-10829.2005
  7. ↑ Agapov EV, Murray CL, Frolov I, Qu L, Myers TM, Rice CM. Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus. J Virol. 2004 Mar;78(5):2414-25. PMID:14963137
  8. ↑ Lecot S, Belouzard S, Dubuisson J, Rouille Y. Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis. J Virol. 2005 Aug;79(16):10826-9. PMID:16051874 doi:10.1128/JVI.79.16.10826-10829.2005
  9. ↑ Agapov EV, Murray CL, Frolov I, Qu L, Myers TM, Rice CM. Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus. J Virol. 2004 Mar;78(5):2414-25. PMID:14963137
  10. ↑ Lecot S, Belouzard S, Dubuisson J, Rouille Y. Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis. J Virol. 2005 Aug;79(16):10826-9. PMID:16051874 doi:10.1128/JVI.79.16.10826-10829.2005
  11. ↑ Agapov EV, Murray CL, Frolov I, Qu L, Myers TM, Rice CM. Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus. J Virol. 2004 Mar;78(5):2414-25. PMID:14963137
  12. ↑ Lecot S, Belouzard S, Dubuisson J, Rouille Y. Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis. J Virol. 2005 Aug;79(16):10826-9. PMID:16051874 doi:10.1128/JVI.79.16.10826-10829.2005
  13. ↑ Agapov EV, Murray CL, Frolov I, Qu L, Myers TM, Rice CM. Uncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus. J Virol. 2004 Mar;78(5):2414-25. PMID:14963137
  14. ↑ Lecot S, Belouzard S, Dubuisson J, Rouille Y. Bovine viral diarrhea virus entry is dependent on clathrin-mediated endocytosis. J Virol. 2005 Aug;79(16):10826-9. PMID:16051874 doi:10.1128/JVI.79.16.10826-10829.2005

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