2lgt

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[[Image:2lgt.jpg|left|200px]]
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==Backbone 1H, 13C, and 15N Chemical Shift Assignments for QFM(Y)F==
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<StructureSection load='2lgt' size='340' side='right' caption='[[2lgt]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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== Structural highlights ==
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[[2lgt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGT OCA]. <br>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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== Publication Abstract from PubMed ==
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Translation termination in eukaryotes is catalyzed by two release factors eRF1 and eRF3 in a cooperative manner. The precise mechanism of stop codon discrimination by eRF1 remains obscure, hindering drug development targeting aberrations at translation termination. By solving the solution structures of the wild-type N-domain of human eRF1 exhibited omnipotent specificity, i.e. recognition of all three stop codons, and its unipotent mutant with UGA-only specificity, we found the conserved GTS loop adopting alternate conformations. We propose that structural variability in the GTS loop may underline the switching between omnipotency and unipotency of eRF1, implying the direct access of the GTS loop to the stop codon. To explore such feasibility, we positioned N-domain in a pre-termination ribosomal complex using the binding interface between N-domain and model RNA oligonucleotides mimicking Helix 44 of 18S rRNA. NMR analysis revealed that those duplex RNA containing 2-nt internal loops interact specifically with helix alpha1 of N-domain, and displace C-domain from a non-covalent complex of N-domain and C-domain, suggesting domain rearrangement in eRF1 that accompanies N-domain accommodation into the ribosomal A site.
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Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1.,Wong LE, Li Y, Pillay S, Frolova L, Pervushin K Nucleic Acids Res. 2012 Mar 1. PMID:22383581<ref>PMID:22383581</ref>
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The line below this paragraph, containing "STRUCTURE_2lgt", creates the "Structure Box" on the page.
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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or leave the SCENE parameter empty for the default display.
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{{STRUCTURE_2lgt| PDB=2lgt | SCENE= }}
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===Backbone 1H, 13C, and 15N Chemical Shift Assignments for QFM(Y)F===
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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== References ==
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<references/>
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__TOC__
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The line below this paragraph, {{ABSTRACT_PUBMED_22383581}}, adds the Publication Abstract to the page
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</StructureSection>
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(as it appears on PubMed at http://www.pubmed.gov), where 22383581 is the PubMed ID number.
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{{ABSTRACT_PUBMED_22383581}}
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==About this Structure==
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[[2lgt]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2LGT OCA].
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==Reference==
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<ref group="xtra">PMID:022383581</ref><references group="xtra"/>
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Li, Y.]]
[[Category: Li, Y.]]

Revision as of 08:39, 30 April 2014

Backbone 1H, 13C, and 15N Chemical Shift Assignments for QFM(Y)F

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