2JYM

Solution structure of stem-loop alpha of the hepatitis B virus post-transcriptional regulatory element


Experimental Data Snapshot

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 15 
  • Selection Criteria: target function 

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This is version 1.2 of the entry. See complete history


Literature

Solution structure of stem-loop alpha of the hepatitis B virus post-transcriptional regulatory element

Schwalbe, M.Ohlenschlager, O.Marchanka, A.Ramachandran, R.Hafner, S.Heise, T.Gorlach, M.

(2008) Nucleic Acids Res 36: 1681-1689

  • DOI: https://doi.org/10.1093/nar/gkn006
  • Primary Citation of Related Structures:  
    2JYM

  • PubMed Abstract: 

    Chronic hepatitis B virus (HBV) infections may lead to severe diseases like liver cirrhosis or hepatocellular carcinoma (HCC). The HBV post-transcriptional regulatory element (HPRE) facilitates the nuclear export of unspliced viral mRNAs, contains a splicing regulatory element and resides in the 3'-region of all viral transcripts. The HPRE consists of three sub-elements alpha (nucleotides 1151-1346), beta1 (nucleotides 1347-1457) and beta2 (nucleotides 1458-1582), which confer together full export competence. Here, we present the NMR solution structure (pdb 2JYM) of the stem-loop alpha (SLalpha, nucleotides 1292-1321) located in the sub-element alpha. The SLalpha contains a CAGGC pentaloop highly conserved in hepatoviruses, which essentially adopts a CUNG-like tetraloop conformation. Furthermore, the SLalpha harbours a single bulged G residue flanked by A-helical regions. The structure is highly suggestive of serving two functions in the context of export of unspliced viral RNA: binding sterile alpha motif (SAM-) domain containing proteins and/or preventing the utilization of a 3'-splice site contained within SLalpha.


  • Organizational Affiliation

    Leibniz-Institut für Altersforschung/Fritz-Lipmann-Institut, Beutenbergstr. 11, D-07745 Jena, Germany.


Macromolecules

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Entity ID: 1
MoleculeChains LengthOrganismImage
RNA (5'-R(*GP*GP*CP*UP*CP*GP*CP*AP*GP*CP*AP*GP*GP*UP*CP*UP*GP*GP*AP*GP*UP*C)-3')22N/A
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: SOLUTION NMR
  • Conformers Calculated: 100 
  • Conformers Submitted: 15 
  • Selection Criteria: target function 

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-04-29
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2022-03-16
    Changes: Database references, Derived calculations