1by0: Difference between revisions

Revision as of 19:53, 30 June 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1by0.png

Template:STRUCTURE 1by0

N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGENN-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN

Template:ABSTRACT PUBMED 10451556

About this StructureAbout this Structure

1BY0 is a Single protein structure. Full experimental information is available from OCA.

ReferenceReference

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 Mon Jun 30 19:53:57 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1by0.gif|left|200px]]
+{{Seed}}
+[[Image:1by0.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1by0|  PDB=1by0  |  SCENE=  }}
-'''N-TERMINAL LEUCINE-REPEAT REGION OF HEPATITIS DELTA ANTIGEN'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_10451556}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 10451556 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_10451556}}
 ==About this Structure==
-BY0 is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY0 OCA].
+BY0 is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BY0 OCA].
 ==Reference==
@@ Line 29: / Line 33: @@
 [[Category: Rna binding]]
 [[Category: Solution structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 12:06:01 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:53:57 2008''