1st4

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{{STRUCTURE_1st4| PDB=1st4 | SCENE= }}
{{STRUCTURE_1st4| PDB=1st4 | SCENE= }}
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'''Structure of DcpS bound to m7GpppA'''
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===Structure of DcpS bound to m7GpppA===
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==Overview==
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Complete removal of residual N-7 guanine cap from degraded messenger RNA is necessary to prevent accumulation of intermediates that might interfere with RNA processing, export, and translation. The human scavenger decapping enzyme, DcpS, catalyzes residual cap hydrolysis following mRNA degradation, releasing N-7 methyl guanosine monophosphate and 5'-diphosphate terminated cap or mRNA products. DcpS structures bound to m(7)GpppG or m(7)GpppA reveal an asymmetric DcpS dimer that simultaneously creates an open nonproductive DcpS-cap complex and a closed productive DcpS-cap complex that alternate via 30 A domain movements. Structural and biochemical analysis suggests an autoregulatory mechanism whereby premature decapping mRNA is prevented by blocking the conformational changes that are required to form a closed productive active site capable of cap hydrolysis.
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{{ABSTRACT_PUBMED_15068804}}
==About this Structure==
==About this Structure==
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[[Category: Mrna]]
[[Category: Mrna]]
[[Category: Rna decay]]
[[Category: Rna decay]]
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Revision as of 12:20, 28 July 2008

Image:1st4.png

Template:STRUCTURE 1st4

Structure of DcpS bound to m7GpppA

Template:ABSTRACT PUBMED 15068804

About this Structure

1ST4 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Insights into the structure, mechanism, and regulation of scavenger mRNA decapping activity., Gu M, Fabrega C, Liu SW, Liu H, Kiledjian M, Lima CD, Mol Cell. 2004 Apr 9;14(1):67-80. PMID:15068804

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