1qgt
From Proteopedia
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| - | [[Image:1qgt.png|left|200px]] | ||
| - | + | ==HUMAN HEPATITIS B VIRAL CAPSID (HBCAG)== | |
| + | <StructureSection load='1qgt' size='340' side='right'caption='[[1qgt]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1qgt]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_B_virus Hepatitis B virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QGT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QGT FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.3Å</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qgt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qgt OCA], [https://pdbe.org/1qgt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qgt RCSB], [https://www.ebi.ac.uk/pdbsum/1qgt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qgt ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q67855_HBV Q67855_HBV] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Hepatitis B is a small enveloped DNA virus that poses a major hazard to human health. The crystal structure of the T = 4 capsid has been solved at 3.3 A resolution, revealing a largely helical protein fold that is unusual for icosahedral viruses. The monomer fold is stabilized by a hydrophobic core that is highly conserved among human viral variants. Association of two amphipathic alpha-helical hairpins results in formation of a dimer with a four-helix bundle as the major central feature. The capsid is assembled from dimers via interactions involving a highly conserved region near the C terminus of the truncated protein used for crystallization. The major immunodominant region lies at the tips of the alpha-helical hairpins that form spikes on the capsid surface. | ||
| - | + | The crystal structure of the human hepatitis B virus capsid.,Wynne SA, Crowther RA, Leslie AG Mol Cell. 1999 Jun;3(6):771-80. PMID:10394365<ref>PMID:10394365</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 1qgt" style="background-color:#fffaf0;"></div> | |
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==See Also== | ==See Also== | ||
| - | *[[Virus coat | + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] |
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| - | [[Category: Hepatitis | + | </StructureSection> |
| - | [[Category: | + | [[Category: Hepatitis B virus]] |
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Crowther RA]] |
| - | [[Category: | + | [[Category: Leslie AGW]] |
| - | + | [[Category: Wynne SA]] | |
| - | + | ||
Current revision
HUMAN HEPATITIS B VIRAL CAPSID (HBCAG)
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