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1m5l

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(New page: 200px<br /> <applet load="1m5l" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m5l" /> '''Structure of wild-type and mutant internal ...)
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<applet load="1m5l" size="450" color="white" frame="true" align="right" spinBox="true"
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'''Structure of wild-type and mutant internal loops from the SL-1 domain of the HIV-1 packaging signal'''<br />
'''Structure of wild-type and mutant internal loops from the SL-1 domain of the HIV-1 packaging signal'''<br />
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==About this Structure==
==About this Structure==
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1M5L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M5L OCA].
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1M5L is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M5L OCA].
==Reference==
==Reference==
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[[Category: sl-1]]
[[Category: sl-1]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:18:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:22:08 2008''

Revision as of 14:22, 15 February 2008


1m5l

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Structure of wild-type and mutant internal loops from the SL-1 domain of the HIV-1 packaging signal

Overview

The packaging signal (Psi) of the human immunodeficiency virus type 1, (HIV-1) enables encapsidation of the full-length genomic RNA against a, background of a vast excess of cellular mRNAs. The core HIV-1 Psi is, approximately 109 nucleotides and contains sequences critical for viral, genomic dimerisation and splicing, in addition to the packaging signal. It, consists of a series of stem-loops (termed SL-1 to SL-4), which can be, arranged in a cloverleaf secondary structure. Using a combination of NMR, spectroscopy, UV melting experiments, molecular modeling and phylogenetic, analyses, we have explored the structure of two conserved internal loops, proximal to the palindromic sequence of SL-1. Internal loop A, composed of, six purines, forms a flexible structure that is strikingly similar to the, Rev responsive element motif when bound to Rev protein. This result, suggests that it may function as a protein-binding site. The absolutely, conserved four-purine internal loop B is instead conformationally and, thermodynamically unstable, and exhibits multiple conformations in, solution. By introducing a double AGG to GGA mutation within this loop, its conformation is stabilised to form a new intra-molecular G:A:G, base-triplet. The structure of the GGA mutant explains the relative, instability of the wild-type loop. In a manner analogous to SL-3, we, propose that conformational flexibility at this site may facilitate, melting of the structure during Gag protein capture or genomic RNA, dimerisation.

About this Structure

1M5L is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

Structure and stability of wild-type and mutant RNA internal loops from the SL-1 domain of the HIV-1 packaging signal., Greatorex J, Gallego J, Varani G, Lever A, J Mol Biol. 2002 Sep 20;322(3):543-57. PMID:12225748

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