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1by0
From Proteopedia
(New page: 200px<br /><applet load="1by0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1by0" /> '''N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITI...) |
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| - | [[Image:1by0.gif|left|200px]]<br /><applet load="1by0" size=" | + | [[Image:1by0.gif|left|200px]]<br /><applet load="1by0" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1by0" /> | caption="1by0" /> | ||
'''N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN'''<br /> | '''N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Hepatitis delta virus (HDV) is a satellite virus of the hepatitis B virus | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1BY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1BY0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY0 OCA]. |
==Reference== | ==Reference== | ||
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10451556 10451556] | 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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10451556 10451556] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cheng, J | + | [[Category: Cheng, J W.]] |
| - | [[Category: Lin, I | + | [[Category: Lin, I J.]] |
| - | [[Category: Lou, Y | + | [[Category: Lou, Y C.]] |
[[Category: helix]] | [[Category: helix]] | ||
[[Category: hepatitis delta antigen]] | [[Category: hepatitis delta antigen]] | ||
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[[Category: solution structure]] | [[Category: solution structure]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:00:23 2008'' |
Revision as of 10:00, 21 February 2008
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N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN
Overview
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.
About this Structure
1BY0 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 12:00:23 2008
