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4che

From Proteopedia

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m (Protected "4che" [edit=sysop:move=sysop])
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'''Unreleased structure'''
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{{STRUCTURE_4che| PDB=4che | SCENE= }}
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===Crystal structure of the putative cap-binding domain of the PB2 subunit of Thogoto virus polymerase===
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{{ABSTRACT_PUBMED_24454773}}
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The entry 4che is ON HOLD
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==Function==
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[[http://www.uniprot.org/uniprot/PB2_THOGV PB2_THOGV]] Initiates transcription by a unique cap-stealing mechanism that involves the cleavage of only the m(7)GpppAm structure from cellular hnRNAs.
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Authors: Guilligay, D., Kadlec, J., Crepin, T., Lunardi, T., Bouvier, D., Kochs, G., Ruigrok, R.W.H., Cusack, S.
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==About this Structure==
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[[4che]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CHE OCA].
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Description: Crystal structure of the putative cap-binding domain of the PB2 subunit of Thogoto virus polymerase
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==Reference==
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<ref group="xtra">PMID:024454773</ref><references group="xtra"/><references/>
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[[Category: Bouvier, D.]]
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[[Category: Crepin, T.]]
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[[Category: Cusack, S.]]
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[[Category: Guilligay, D.]]
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[[Category: Kadlec, J.]]
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[[Category: Kochs, G.]]
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[[Category: Lunardi, T.]]
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[[Category: Ruigrok, R W.H.]]
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[[Category: Viral protein]]

Revision as of 11:06, 5 February 2014

Template:STRUCTURE 4che

Contents

Crystal structure of the putative cap-binding domain of the PB2 subunit of Thogoto virus polymerase

Template:ABSTRACT PUBMED 24454773

Function

[PB2_THOGV] Initiates transcription by a unique cap-stealing mechanism that involves the cleavage of only the m(7)GpppAm structure from cellular hnRNAs.

About this Structure

4che is a 1 chain structure. Full crystallographic information is available from OCA.

Reference

  • Guilligay D, Kadlec J, Crepin T, Lunardi T, Bouvier D, Kochs G, Ruigrok RW, Cusack S. Comparative structural and functional analysis of orthomyxovirus polymerase cap-snatching domains. PLoS One. 2014 Jan 15;9(1):e84973. doi: 10.1371/journal.pone.0084973. eCollection, 2014 Jan 15. PMID:24454773 doi:http://dx.doi.org/10.1371/journal.pone.0084973

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