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4k6m

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'''Unreleased structure'''
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{{STRUCTURE_4k6m| PDB=4k6m | SCENE= }}
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===Crystal Structure of the full-length Japanese encephalitis virus NS5===
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The entry 4k6m is ON HOLD until Paper Publication
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==Function==
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[[http://www.uniprot.org/uniprot/Q5NT71_9FLAV Q5NT71_9FLAV]] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS000336_004_099774]
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Authors: Lu, G., Gong, P.
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==About this Structure==
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[[4k6m]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Japanese_encephalitis_virus Japanese encephalitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4K6M OCA].
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Description: Crystal Structure of the full-length Japanese encephalitis virus NS5
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[[Category: Japanese encephalitis virus]]
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[[Category: Gong, P.]]
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[[Category: Lu, G.]]
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[[Category: Methyltransferase]]
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[[Category: Rna-dependent rna polymerase]]
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[[Category: Transferase]]

Revision as of 07:39, 28 August 2013

Template:STRUCTURE 4k6m

Crystal Structure of the full-length Japanese encephalitis virus NS5

Function

[Q5NT71_9FLAV] Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).[SAAS:SAAS000336_004_099774]

About this Structure

4k6m is a 2 chain structure with sequence from Japanese encephalitis virus. Full crystallographic information is available from OCA.

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OCA

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