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PMID: 9707559 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

A 1.3-A resolution crystal structure of the HIV-1 trans-activation response region RNA stem reveals a metal ion-dependent bulge conformation.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 95 ·No. 17 ·1998-08-18 ·Pages 9819-24

Ippolito JA, Steitz TA

Abstract

The crystal structure of an HIV-1 trans-activation response region (TAR) RNA fragment containing the binding site for the trans-activation protein Tat has been determined to 1.3-A resolution. In this crystal structure, the characteristic UCU bulge of TAR adopts a conformation that is stabilized by three divalent calcium ions and differs from those determined previously by solution NMR. One metal ion, crucial to the loop conformation, binds directly to three phosphates in the loop region. The structure emphasizes the influence of metal ion binding on RNA structure and, given the abundance of divalent metal ion in the cell, raises the question of whether metal ions play a role in the conformation of TAR RNA and the interaction of TAR with Tat and cyclin T in vivo.

MeSH Terms
Base Sequence Binding Sites Calcium/metabolism Crystallography, X-Ray HIV-1/chemistry,genetics,metabolism Magnesium/metabolism Magnetic Resonance Spectroscopy Models, Molecular Nucleic Acid Conformation RNA, Viral/chemistry,genetics,metabolism Transcriptional Activation
Chemicals
RNA, Viral Magnesium Calcium
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Ippolito J A
Department of Molecular Biophysics and Biochemistry,, New Haven, CT 06520-8114, USA.
Steitz T A
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.95.17.9819
Published
1998-08-18
Pages
9819-24
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC21420
Subset
IM
Grants
NIGMS NIH HHS · F32 GM017645 · United States
NIGMS NIH HHS · GM17645 · United States
NIGMS NIH HHS · GM39546 · United States
External Links
PubMed source DOI: 10.1073/pnas.95.17.9819 PMC Full Text View journal details
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