2a19: Difference between revisions

Revision as of 00:56, 28 July 2008

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File:2a19.png

Template:STRUCTURE 2a19

PKR kinase domain- eIF2alpha- AMP-PNP complex.PKR kinase domain- eIF2alpha- AMP-PNP complex.

Template:ABSTRACT PUBMED 16179258

About this StructureAbout this Structure

2A19 is a Protein complex structure of sequences from Homo sapiens and Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

ReferenceReference

Higher-order substrate recognition of eIF2alpha by the RNA-dependent protein kinase PKR., Dar AC, Dever TE, Sicheri F, Cell. 2005 Sep 23;122(6):887-900. PMID:16179258

Page seeded by OCA on Mon Jul 28 00:56:35 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2a19.gif|left|200px]]
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-'''PKR kinase domain- eIF2alpha- AMP-PNP complex.'''
+===PKR kinase domain- eIF2alpha- AMP-PNP complex.===
-==Overview==
+<!--
-In response to binding viral double-stranded RNA byproducts within a cell, the RNA-dependent protein kinase PKR phosphorylates the alpha subunit of the translation initiation factor eIF2 on a regulatory site, Ser51. This triggers the general shutdown of protein synthesis and inhibition of viral propagation. To understand the basis for substrate recognition by and the regulation of PKR, we determined X-ray crystal structures of the catalytic domain of PKR in complex with eIF2alpha. The structures reveal that eIF2alpha binds to the C-terminal catalytic lobe while catalytic-domain dimerization is mediated by the N-terminal lobe. In addition to inducing a local unfolding of the Ser51 acceptor site in eIF2alpha, its mode of binding to PKR affords the Ser51 site full access to the catalytic cleft of PKR. The generality and implications of the structural mechanisms uncovered for PKR to the larger family of four human eIF2alpha protein kinases are discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_16179258}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16179258 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16179258}}
 ==About this Structure==
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 [[Category: Protein biosynthesis]]
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