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==N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN== | |||
<StructureSection load='1by0' size='340' side='right'caption='[[1by0]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1by0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hepatitis_delta_virus_(ISOLATE_AMERICAN) Hepatitis delta virus (ISOLATE AMERICAN)]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BY0 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1by0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by0 OCA], [https://pdbe.org/1by0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1by0 RCSB], [https://www.ebi.ac.uk/pdbsum/1by0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1by0 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
''' | [https://www.uniprot.org/uniprot/SHDAG_HDVAM SHDAG_HDVAM] Promotes both transcription and replication of genomic RNA. Following virus entry into host cell, provides nuclear import of HDV RNPs thanks to its nuclear localization signal. May interact with host RNA polymerase II thereby changing its template requirement from DNA to RNA. RNA pol II complex would then acts as an RNA-directed RNA polymerase, and transcribe and replicate HDV genome (By similarity). | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
== | |||
Hepatitis delta virus (HDV) is a satellite virus of the hepatitis B virus (HBV) which provides the surface antigen for the viral coat. The RNA genome of HDV encodes two proteins: the small delta antigen and the large delta antigen. The two proteins resemble each other except for the presence of an additional 19 amino acids at the C terminus of the latter species. We have found that the N-terminal leucine-repeat region of hepatitis delta antigen (HDAg) binds to the autolytic domain of HDV genomic RNA and attenuates its autolytic activity. A 27-residue polypeptide corresponding to residues 24-50 of HDAg, designated dAg(24-50), was synthesized, and its solution structure was found to be an alpha-helix by circular dichroism and (1)H-nuclear magnetic resonance (NMR) techniques. Binding affinity of dAg(24-50) with HDV genomic RNA was found to increase with its alpha-helical content, and it was further confirmed by modifying its N- and C-terminal groups. Furthermore, the absence of RNA binding activity in the mutant peptides, dAgM(24-50am) and dAgM(Ac24-50am), in which Lys38, Lys39, and Lys40 were changed to Glu, indicates a possible involvement of these residues in their binding activity. Structural knowledge of the N-terminal leucine-repeat region of HDAg thus provides a molecular basis for the understanding of its role in the interaction with RNA. Proteins 1999;37:121-129. | Hepatitis delta virus (HDV) is a satellite virus of the hepatitis B virus (HBV) which provides the surface antigen for the viral coat. The RNA genome of HDV encodes two proteins: the small delta antigen and the large delta antigen. The two proteins resemble each other except for the presence of an additional 19 amino acids at the C terminus of the latter species. We have found that the N-terminal leucine-repeat region of hepatitis delta antigen (HDAg) binds to the autolytic domain of HDV genomic RNA and attenuates its autolytic activity. A 27-residue polypeptide corresponding to residues 24-50 of HDAg, designated dAg(24-50), was synthesized, and its solution structure was found to be an alpha-helix by circular dichroism and (1)H-nuclear magnetic resonance (NMR) techniques. Binding affinity of dAg(24-50) with HDV genomic RNA was found to increase with its alpha-helical content, and it was further confirmed by modifying its N- and C-terminal groups. Furthermore, the absence of RNA binding activity in the mutant peptides, dAgM(24-50am) and dAgM(Ac24-50am), in which Lys38, Lys39, and Lys40 were changed to Glu, indicates a possible involvement of these residues in their binding activity. Structural knowledge of the N-terminal leucine-repeat region of HDAg thus provides a molecular basis for the understanding of its role in the interaction with RNA. Proteins 1999;37:121-129. | ||
Solution structure and RNA-binding activity of the N-terminal leucine-repeat region of hepatitis delta antigen.,Lin IJ, Lou YC, Pai MT, Wu HN, Cheng JW Proteins. 1999 Oct 1;37(1):121-9. PMID:10451556<ref>PMID:10451556</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
[[Category: | <div class="pdbe-citations 1by0" style="background-color:#fffaf0;"></div> | ||
[[Category: Cheng | == References == | ||
[[Category: Lin | <references/> | ||
[[Category: Lou | __TOC__ | ||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Cheng JW]] | |||
[[Category: Lin IJ]] | |||
[[Category: Lou YC]] | |||
Latest revision as of 14:37, 22 November 2023
N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGENN-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN
Structural highlights
FunctionSHDAG_HDVAM Promotes both transcription and replication of genomic RNA. Following virus entry into host cell, provides nuclear import of HDV RNPs thanks to its nuclear localization signal. May interact with host RNA polymerase II thereby changing its template requirement from DNA to RNA. RNA pol II complex would then acts as an RNA-directed RNA polymerase, and transcribe and replicate HDV genome (By similarity). Publication Abstract from PubMedHepatitis delta virus (HDV) is a satellite virus of the hepatitis B virus (HBV) which provides the surface antigen for the viral coat. The RNA genome of HDV encodes two proteins: the small delta antigen and the large delta antigen. The two proteins resemble each other except for the presence of an additional 19 amino acids at the C terminus of the latter species. We have found that the N-terminal leucine-repeat region of hepatitis delta antigen (HDAg) binds to the autolytic domain of HDV genomic RNA and attenuates its autolytic activity. A 27-residue polypeptide corresponding to residues 24-50 of HDAg, designated dAg(24-50), was synthesized, and its solution structure was found to be an alpha-helix by circular dichroism and (1)H-nuclear magnetic resonance (NMR) techniques. Binding affinity of dAg(24-50) with HDV genomic RNA was found to increase with its alpha-helical content, and it was further confirmed by modifying its N- and C-terminal groups. Furthermore, the absence of RNA binding activity in the mutant peptides, dAgM(24-50am) and dAgM(Ac24-50am), in which Lys38, Lys39, and Lys40 were changed to Glu, indicates a possible involvement of these residues in their binding activity. Structural knowledge of the N-terminal leucine-repeat region of HDAg thus provides a molecular basis for the understanding of its role in the interaction with RNA. Proteins 1999;37:121-129. Solution structure and RNA-binding activity of the N-terminal leucine-repeat region of hepatitis delta antigen.,Lin IJ, Lou YC, Pai MT, Wu HN, Cheng JW Proteins. 1999 Oct 1;37(1):121-9. PMID:10451556[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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