2btl: Difference between revisions
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[[Image:2btl.gif|left|200px]] | [[Image:2btl.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF IBV CORONAVIRUS NUCLEOCAPSID''' | {{Structure | ||
|PDB= 2btl |SIZE=350|CAPTION= <scene name='initialview01'>2btl</scene>, resolution 1.95Å | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
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'''CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF IBV CORONAVIRUS NUCLEOCAPSID''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2BTL is a [ | 2BTL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Infectious_bronchitis_virus Infectious bronchitis virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BTL OCA]. | ||
==Reference== | ==Reference== | ||
The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties., Fan H, Ooi A, Tan YW, Wang S, Fang S, Liu DX, Lescar J, Structure. 2005 Dec;13(12):1859-68. PMID:[http:// | The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties., Fan H, Ooi A, Tan YW, Wang S, Fang S, Liu DX, Lescar J, Structure. 2005 Dec;13(12):1859-68. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16338414 16338414] | ||
[[Category: Infectious bronchitis virus]] | [[Category: Infectious bronchitis virus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: viral nucleoprotein]] | [[Category: viral nucleoprotein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:06:31 2008'' | ||
Revision as of 14:06, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF THE N-TERMINAL DOMAIN OF IBV CORONAVIRUS NUCLEOCAPSID
Overview
The coronavirus nucleocapsid (N) protein packages viral genomic RNA into a ribonucleoprotein complex. Interactions between N proteins and RNA are thus crucial for the assembly of infectious virus particles. The 45 kDa recombinant nucleocapsid N protein of coronavirus infectious bronchitis virus (IBV) is highly sensitive to proteolysis. We obtained a stable fragment of 14.7 kDa spanning its N-terminal residues 29-160 (IBV-N29-160). Like the N-terminal RNA binding domain (SARS-N45-181) of the severe acute respiratory syndrome virus (SARS-CoV) N protein, the crystal structure of the IBV-N29-160 fragment at 1.85 A resolution reveals a protein core composed of a five-stranded antiparallel beta sheet with a positively charged beta hairpin extension and a hydrophobic platform that are probably involved in RNA binding. Crosslinking studies demonstrate the formation of dimers, tetramers, and higher multimers of IBV-N. A model for coronavirus shell formation is proposed in which dimerization of the C-terminal domain of IBV-N leads to oligomerization of the IBV-nucleocapsid protein and viral RNA condensation.
About this Structure
2BTL is a Single protein structure of sequence from Infectious bronchitis virus. Full crystallographic information is available from OCA.
Reference
The nucleocapsid protein of coronavirus infectious bronchitis virus: crystal structure of its N-terminal domain and multimerization properties., Fan H, Ooi A, Tan YW, Wang S, Fang S, Liu DX, Lescar J, Structure. 2005 Dec;13(12):1859-68. PMID:16338414
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