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[[ | ==N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN== | ||
<StructureSection load='1by0' size='340' side='right' caption='[[1by0]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1by0]] is a 1 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1BY0 FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1by0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1by0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1by0 RCSB], [http://www.ebi.ac.uk/pdbsum/1by0 PDBsum]</span></td></tr> | |||
<table> | |||
<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. | |||
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> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
< | |||
[[Category: Cheng, J W.]] | [[Category: Cheng, J W.]] | ||
[[Category: Lin, I J.]] | [[Category: Lin, I J.]] | ||
Revision as of 08:36, 8 June 2014
N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGENN-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN
Structural highlights
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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