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2qij

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Revision as of 08:30, 12 October 2017

Hepatitis B Capsid Protein with an N-terminal extension modelled into 8.9 A data.

Structural highlights

2qij is a 4 chain structure with sequence from Hbv-d. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	1qgt, 2g34, 2g33
Gene:	C (HBV-D)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Hepatitis B core (HBc) particles have been extensively exploited as carriers for foreign immunological epitopes in the development of multicomponent vaccines and diagnostic reagents. Crystals of the T = 4 HBc particle were grown in PEG 20,000, ammonium sulfate and various types of alcohols. A temperature jump from 277 or 283 to 290 K was found to enhance crystal growth. A crystal grown using MPD as a cryoprotectant diffracted X-rays to 7.7 A resolution and data were collected to 99.6% completeness at 8.9 A. The crystal belongs to space group P2(1)2(1)2(1), with unit-cell parameters a = 352.3, b = 465.5, c = 645.0 A. The electron-density map reveals a protrusion that is consistent with the N-terminus extending out from the surface of the capsid. The structure presented here supports the idea that N-terminal insertions can be exploited in the development of diagnostic reagents, multicomponent vaccines and delivery vehicles into mammalian cells.

Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension.,Tan WS, McNae IW, Ho KL, Walkinshaw MD Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):642-7. Epub 2007 Jul 21. PMID:17671358^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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
↑ Tan WS, McNae IW, Ho KL, Walkinshaw MD. Crystallization and X-ray analysis of the T = 4 particle of hepatitis B capsid protein with an N-terminal extension. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Aug 1;63(Pt, 8):642-7. Epub 2007 Jul 21. PMID:17671358 doi:10.1107/S1744309107033726

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2qij"

@@ Line 1: / Line 1: @@
 ==Hepatitis B Capsid Protein with an N-terminal extension modelled into 8.9 A data.==
 <StructureSection load='2qij' size='340' side='right' caption='[[2qij]], [[Resolution|resolution]] 8.90&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qgt|1qgt]], [[2g34|2g34]], [[2g33|2g33]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10419 HBV-D])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qij OCA], [http://pdbe.org/2qij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qij RCSB], [http://www.ebi.ac.uk/pdbsum/2qij PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2qij FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qij OCA], [http://pdbe.org/2qij PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qij RCSB], [http://www.ebi.ac.uk/pdbsum/2qij PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qij ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 2qij" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Virus coat protein|Virus coat protein]]
 == References ==
 <references/>

2qij

From Proteopedia

Revision as of 08:30, 12 October 2017

Hepatitis B Capsid Protein with an N-terminal extension modelled into 8.9 A data.

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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