1wz4

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(Difference between revisions)

Revision as of 16:30, 27 October 2021

Solution Conformation of adr subtype HBV Pre-S2 Epitope

Structural highlights

1wz4 is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[HBSAG_HBVC5] The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assumes fusion between virion membrane and endosomal membrane (Probable). In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein (By similarity). The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid (By similarity).

Publication Abstract from PubMed

We have determined the solution conformation of the major B cell epitope (residues 123-145, adrl23 hereafter) in the preS2 region of hepatitis B virus known to be associated with infection neutralization. The adrl23 shows an "L" shaped helix-turn-helix topology with two beta-turns formed by residues Ala(130)-Asp(133) and Asp(133)-Val(136) intervening the N- and C-terminal helices. The N-terminal alpha-helix consists of residues Ser(124)-Gln(129) whereas the C-terminal 3(10) helix is formed by residues Val(136)-Tyr(140). The beta-turns overlap partially with the putative "conformational" epitope. The overall topology of adrl23 is primarily maintained by hydrophobic interactions involving Phe(127), Leu(131), Leu(132), Val(136), and Tyr(140) that are clustered on one side of the molecule. An additional hydrophobic stabilization comes from Phe(141) that is buried inside the concave side of the molecule. A network of hydrogen bonds formed among Thr(125), His(128), and Arg(137) further contribute to the "boomerang-shaped" architecture of adrl23. The N-terminus of adrl23 is immobile due to a hydrogen bond between the N-terminal amide proton of Asn(123) and the hydroxyl oxygen of Thr(126). The side chains of Asp(133), Arg(135), Val(136), Leu(139), and Tyr(140) that were shown to be important for binding to a monoclonal antibody H8 mAb are surface exposed.

Solution conformation of an immunodominant epitope in the hepatitis B virus preS2 surface antigen.,Chi SW, Kim DH, Kim JS, Lee MK, Han KH Antiviral Res. 2006 Dec;72(3):207-15. Epub 2006 Jul 7. PMID:16872688^[1]

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

References

↑ Chi SW, Kim DH, Kim JS, Lee MK, Han KH. Solution conformation of an immunodominant epitope in the hepatitis B virus preS2 surface antigen. Antiviral Res. 2006 Dec;72(3):207-15. Epub 2006 Jul 7. PMID:16872688 doi:10.1016/j.antiviral.2006.06.009

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

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OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wz4"

Categories: Large Structures | Chi, S W | Han, K H | Gene regulation | Helix turn helix

@@ Line 3: / Line 3: @@
 <StructureSection load='1wz4' size='340' side='right'caption='[[1wz4]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1wz4]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ4 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1WZ4 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1wz4]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WZ4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WZ4 FirstGlance]. <br>
-</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=1wz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wz4 OCA], [http://pdbe.org/1wz4 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wz4 RCSB], [http://www.ebi.ac.uk/pdbsum/1wz4 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1wz4 ProSAT]</span></td></tr>
+</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=1wz4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wz4 OCA], [https://pdbe.org/1wz4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wz4 RCSB], [https://www.ebi.ac.uk/pdbsum/1wz4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wz4 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/HBSAG_HBVC5 HBSAG_HBVC5]] The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assumes fusion between virion membrane and endosomal membrane (Probable). In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein (By similarity).  The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid (By similarity).
+[[https://www.uniprot.org/uniprot/HBSAG_HBVC5 HBSAG_HBVC5]] The large envelope protein exists in two topological conformations, one which is termed 'external' or Le-HBsAg and the other 'internal' or Li-HBsAg. In its external conformation the protein attaches the virus to cell receptors and thereby initiating infection. This interaction determines the species specificity and liver tropism. This attachment induces virion internalization predominantly through caveolin-mediated endocytosis. The large envelope protein also assumes fusion between virion membrane and endosomal membrane (Probable). In its internal conformation the protein plays a role in virion morphogenesis and mediates the contact with the nucleocapsid like a matrix protein (By similarity).  The middle envelope protein plays an important role in the budding of the virion. It is involved in the induction of budding in a nucleocapsid independent way. In this process the majority of envelope proteins bud to form subviral lipoprotein particles of 22 nm of diameter that do not contain a nucleocapsid (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

1wz4

From Proteopedia

Revision as of 16:30, 27 October 2021

Solution Conformation of adr subtype HBV Pre-S2 Epitope

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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