1csl

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==Overview==
==Overview==
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The crystal structure of a 28 nt RNA fragment containing the human, immunodeficiency virus type 1 (HIV-1) Rev response element high affinity, binding site for Rev protein has been solved at 1.6 A resolution. The, overall structure of the RRE helix is greatly distorted from A-form, geometry by the presence of two purine-purine base-pairs and two single, nucleotide bulges. G48 and G71 form a Hoogsteen-type asymmetric base-pair, with G71 adopting a syn conformation. The non-canonical regions in the, unliganded Rev response element molecule narrow the major groove width, with respect to standard A-RNA. The Rev response element structure, observed here represents a closed form of the Rev binding site and differs, from conformations of the RNA observed previously by solution NMR studies.
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The crystal structure of a 28 nt RNA fragment containing the human immunodeficiency virus type 1 (HIV-1) Rev response element high affinity binding site for Rev protein has been solved at 1.6 A resolution. The overall structure of the RRE helix is greatly distorted from A-form geometry by the presence of two purine-purine base-pairs and two single nucleotide bulges. G48 and G71 form a Hoogsteen-type asymmetric base-pair with G71 adopting a syn conformation. The non-canonical regions in the unliganded Rev response element molecule narrow the major groove width with respect to standard A-RNA. The Rev response element structure observed here represents a closed form of the Rev binding site and differs from conformations of the RNA observed previously by solution NMR studies.
==About this Structure==
==About this Structure==
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The structure of the HIV-1 RRE high affinity rev binding site at 1.6 A resolution., Ippolito JA, Steitz TA, J Mol Biol. 2000 Jan 28;295(4):711-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10656783 10656783]
The structure of the HIV-1 RRE high affinity rev binding site at 1.6 A resolution., Ippolito JA, Steitz TA, J Mol Biol. 2000 Jan 28;295(4):711-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10656783 10656783]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Ippolito, J.A.]]
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[[Category: Ippolito, J A.]]
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[[Category: Steitz, T.A.]]
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[[Category: Steitz, T A.]]
[[Category: hiv-1]]
[[Category: hiv-1]]
[[Category: rre high affinity site]]
[[Category: rre high affinity site]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:37:01 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:20 2008''

Revision as of 10:09, 21 February 2008


1csl, resolution 1.60Å

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CRYSTAL STRUCTURE OF THE RRE HIGH AFFINITY SITE

Overview

The crystal structure of a 28 nt RNA fragment containing the human immunodeficiency virus type 1 (HIV-1) Rev response element high affinity binding site for Rev protein has been solved at 1.6 A resolution. The overall structure of the RRE helix is greatly distorted from A-form geometry by the presence of two purine-purine base-pairs and two single nucleotide bulges. G48 and G71 form a Hoogsteen-type asymmetric base-pair with G71 adopting a syn conformation. The non-canonical regions in the unliganded Rev response element molecule narrow the major groove width with respect to standard A-RNA. The Rev response element structure observed here represents a closed form of the Rev binding site and differs from conformations of the RNA observed previously by solution NMR studies.

About this Structure

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

Reference

The structure of the HIV-1 RRE high affinity rev binding site at 1.6 A resolution., Ippolito JA, Steitz TA, J Mol Biol. 2000 Jan 28;295(4):711-7. PMID:10656783

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