2gjk

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(New page: 200px<br /> <applet load="2gjk" size="450" color="white" frame="true" align="right" spinBox="true" caption="2gjk, resolution 2.60&Aring;" /> '''Structural and func...)
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caption="2gjk, resolution 2.60&Aring;" />
caption="2gjk, resolution 2.60&Aring;" />
'''Structural and functional insights into the human Upf1 helicase core'''<br />
'''Structural and functional insights into the human Upf1 helicase core'''<br />
==Overview==
==Overview==
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Nonsense-mediated mRNA decay (NMD) is an mRNA surveillance pathway that, recognizes and degrades aberrant mRNAs containing premature stop codons. A, critical protein in NMD is Upf1p, which belongs to the helicase super, family 1 (SF1), and is thought to utilize the energy of ATP hydrolysis to, promote transitions in the structure of RNA or RNA-protein complexes. The, crystal structure of the catalytic core of human Upf1p determined in three, states (phosphate-, AMPPNP- and ADP-bound forms) reveals an overall, structure containing two RecA-like domains with two additional domains, protruding from the N-terminal RecA-like domain. Structural comparison, combined with mutational analysis identifies a likely single-stranded RNA, (ssRNA)-binding channel, and a cycle of conformational change coupled to, ATP binding and hydrolysis. These conformational changes alter the likely, ssRNA-binding channel in a manner that can explain how ATP binding, destabilizes ssRNA binding to Upf1p.
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Nonsense-mediated mRNA decay (NMD) is an mRNA surveillance pathway that recognizes and degrades aberrant mRNAs containing premature stop codons. A critical protein in NMD is Upf1p, which belongs to the helicase super family 1 (SF1), and is thought to utilize the energy of ATP hydrolysis to promote transitions in the structure of RNA or RNA-protein complexes. The crystal structure of the catalytic core of human Upf1p determined in three states (phosphate-, AMPPNP- and ADP-bound forms) reveals an overall structure containing two RecA-like domains with two additional domains protruding from the N-terminal RecA-like domain. Structural comparison combined with mutational analysis identifies a likely single-stranded RNA (ssRNA)-binding channel, and a cycle of conformational change coupled to ATP binding and hydrolysis. These conformational changes alter the likely ssRNA-binding channel in a manner that can explain how ATP binding destabilizes ssRNA binding to Upf1p.
==About this Structure==
==About this Structure==
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2GJK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and ANP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2GJK OCA].
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2GJK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=ANP:'>ANP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GJK OCA].
==Reference==
==Reference==
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[[Category: nmd]]
[[Category: nmd]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:19:21 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:32:19 2008''

Revision as of 15:32, 21 February 2008

Image:2gjk.gif

2gjk, resolution 2.60Å

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Structural and functional insights into the human Upf1 helicase core

Overview

Nonsense-mediated mRNA decay (NMD) is an mRNA surveillance pathway that recognizes and degrades aberrant mRNAs containing premature stop codons. A critical protein in NMD is Upf1p, which belongs to the helicase super family 1 (SF1), and is thought to utilize the energy of ATP hydrolysis to promote transitions in the structure of RNA or RNA-protein complexes. The crystal structure of the catalytic core of human Upf1p determined in three states (phosphate-, AMPPNP- and ADP-bound forms) reveals an overall structure containing two RecA-like domains with two additional domains protruding from the N-terminal RecA-like domain. Structural comparison combined with mutational analysis identifies a likely single-stranded RNA (ssRNA)-binding channel, and a cycle of conformational change coupled to ATP binding and hydrolysis. These conformational changes alter the likely ssRNA-binding channel in a manner that can explain how ATP binding destabilizes ssRNA binding to Upf1p.

About this Structure

2GJK is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.

Reference

Structural and functional insights into the human Upf1 helicase core., Cheng Z, Muhlrad D, Lim MK, Parker R, Song H, EMBO J. 2007 Jan 10;26(1):253-64. Epub 2006 Dec 7. PMID:17159905

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