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484d

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[[Image:484d.gif|left|200px]]
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{{Seed}}
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[[Image:484d.png|left|200px]]
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{{STRUCTURE_484d| PDB=484d | SCENE= }}
{{STRUCTURE_484d| PDB=484d | SCENE= }}
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'''SOLUTION STRUCTURE OF HIV-1 REV PEPTIDE-RNA APTAMER COMPLEX'''
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===SOLUTION STRUCTURE OF HIV-1 REV PEPTIDE-RNA APTAMER COMPLEX===
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==Overview==
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BACKGROUND: The biological function of several viral and bacteriophage proteins, and their arginine-rich subdomains, involves RNA-mediated interactions. It has been shown recently that bound peptides adopt either beta-hairpin or alpha-helical conformations in viral and phage peptide-RNA complexes. We have compared the structures of the arginine-rich peptide domain of HIV-1 Rev bound to two RNA aptamers to determine whether RNA architecture can dictate the conformations of a bound peptide. RESULTS: The core-binding segment of the HIV-1 Rev peptide class II RNA aptamer complex spans the two-base bulge and hairpin loop of the bound RNA and the carboxy-terminal segment of the bound peptide. The bound peptide is anchored in place by backbone and sidechain intermolecular hydrogen bonding and van der Waals stacking interactions. One of the bulge bases participates in U*(A*U) base triple formation, whereas the other is looped out and flaps over the bound peptide in the complex. The seven-residue hairpin loop is closed by a sheared G*A mismatch pair with several pyrimidines looped out of the hairpin fold. CONCLUSIONS: Our structural studies establish that RNA architecture dictates whether the same HIV-1 Rev peptide folds into an extended or alpha-helical conformation on complex formation. Arginine-rich peptides can therefore adapt distinct secondary folds to complement the tertiary folds of their RNA targets. This contrasts with protein-RNA complexes in which elements of RNA secondary structure adapt to fit within the tertiary folds of their protein targets.
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The line below this paragraph, {{ABSTRACT_PUBMED_10467126}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 10467126 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10467126}}
==About this Structure==
==About this Structure==
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484D is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=484D OCA].
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484D is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=484D OCA].
==Reference==
==Reference==
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[[Category: Rna aptamer]]
[[Category: Rna aptamer]]
[[Category: Tertiary architecture]]
[[Category: Tertiary architecture]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 22:19:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 3 13:26:08 2008''

Revision as of 10:26, 3 July 2008

Image:484d.png

Template:STRUCTURE 484d

SOLUTION STRUCTURE OF HIV-1 REV PEPTIDE-RNA APTAMER COMPLEX

Template:ABSTRACT PUBMED 10467126

About this Structure

484D is a Single protein structure. Full experimental information is available from OCA.

Reference

RNA architecture dictates the conformations of a bound peptide., Ye X, Gorin A, Frederick R, Hu W, Majumdar A, Xu W, McLendon G, Ellington A, Patel DJ, Chem Biol. 1999 Sep;6(9):657-69. PMID:10467126

Page seeded by OCA on Thu Jul 3 13:26:08 2008

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