4bmg
From Proteopedia
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{{STRUCTURE_4bmg| PDB=4bmg | SCENE= }} | {{STRUCTURE_4bmg| PDB=4bmg | SCENE= }} | ||
===Crystal structure of hexameric HBc149 Y132A=== | ===Crystal structure of hexameric HBc149 Y132A=== | ||
| + | {{ABSTRACT_PUBMED_23824290}} | ||
==Function== | ==Function== | ||
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==Reference== | ==Reference== | ||
| - | <references group="xtra"/><references/> | + | <ref group="xtra">PMID:023824290</ref><references group="xtra"/><references/> |
[[Category: Hepatitis b virus]] | [[Category: Hepatitis b virus]] | ||
[[Category: Alexander, C G.]] | [[Category: Alexander, C G.]] | ||
Revision as of 04:36, 18 July 2013
Contents |
Crystal structure of hexameric HBc149 Y132A
Template:ABSTRACT PUBMED 23824290
Function
[CAPSD_HBVD1] Self assembles to form an icosahedral capsid. Most capsid appear to be large particles with a icosahedral symmetry of T=4 and consist of 240 copies of capsid protein, though a fraction forms smaller T=3 particles consisting of 180 capsid proteins. Entering capsid are transported along microtubules to the nucleus. Phosphorylation of the capsid is thought to induce exposure of nuclear localization signal in the C-terminal portion of the capsid protein that allows binding to the nuclear pore complex via the importin (karyopherin-) alpha and beta. Capsids are imported in intact form through the nuclear pore into the nuclear basket, where it probably binds NUP153. Only capsids that contain the mature viral genome can release the viral DNA and capsid protein into the nucleoplasm. Immature capsids get stucked in the basket. Capsids encapsulate the pre-genomic RNA and the P protein. Pre-genomic RNA is reverse transcribed into DNA while the capsid is still in the cytoplasm. The capsid can then either be directed to the nucleus, providing more genome for transcription, or bud through the endoplasmic reticulum to provide new virions (By similarity).[1] Encapsidates hepatitis delta genome (By similarity).[2]
About this Structure
4bmg is a 6 chain structure with sequence from Hepatitis b virus. Full crystallographic information is available from OCA.
Reference
- Alexander CG, Jurgens MC, Shepherd DA, Freund SM, Ashcroft AE, Ferguson N. Thermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core protein. Proc Natl Acad Sci U S A. 2013 Jul 3. PMID:23824290 doi:10.1073/pnas.1308846110
- ↑ Wingfield PT, Stahl SJ, Williams RW, Steven AC. Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry. 1995 Apr 18;34(15):4919-32. PMID:7711014
- ↑ Wingfield PT, Stahl SJ, Williams RW, Steven AC. Hepatitis core antigen produced in Escherichia coli: subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry. 1995 Apr 18;34(15):4919-32. PMID:7711014
