<table><tr><td colspan='2'>[[3j92]] is a 55 chain structure with sequence from [http://en.wikipedia.org/wiki/European_rabbit European rabbit], [http://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J92 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=3J92 FirstGlance]. <br>
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<table><tr><td colspan='2'>[[3j92]] is a 55 chain structure with sequence from [https://en.wikipedia.org/wiki/European_rabbit European rabbit], [https://en.wikipedia.org/wiki/Oryctolagus_cuniculus Oryctolagus cuniculus] and [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3J92 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3J92 FirstGlance]. <br>
[[http://www.uniprot.org/uniprot/NEMF_HUMAN NEMF_HUMAN]] Plays a role in nuclear export.<ref>PMID:16103875</ref> [[http://www.uniprot.org/uniprot/LTN1_HUMAN LTN1_HUMAN]] E3 ubiquitin-protein ligase. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity).
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[[https://www.uniprot.org/uniprot/NEMF_HUMAN NEMF_HUMAN]] Plays a role in nuclear export.<ref>PMID:16103875</ref> [[https://www.uniprot.org/uniprot/LTN1_HUMAN LTN1_HUMAN]] E3 ubiquitin-protein ligase. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity).
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
Revision as of 13:28, 4 May 2022
Structure and assembly pathway of the ribosome quality control complex
[NEMF_HUMAN] Plays a role in nuclear export.[1] [LTN1_HUMAN] E3 ubiquitin-protein ligase. E3 ubiquitin ligases accept ubiquitin from an E2 ubiquitin-conjugating enzyme in the form of a thioester and then directly transfer the ubiquitin to targeted substrates (By similarity).
Publication Abstract from PubMed
During ribosome-associated quality control, stalled ribosomes are split into subunits and the 60S-housed nascent polypeptides are poly-ubiquitinated by Listerin. How this low-abundance ubiquitin ligase targets rare stall-generated 60S among numerous empty 60S is unknown. Here, we show that Listerin specificity for nascent chain-60S complexes depends on nuclear export mediator factor (NEMF). The 3.6 A cryo-EM structure of a nascent chain-containing 60S-Listerin-NEMF complex revealed that NEMF makes multiple simultaneous contacts with 60S and peptidyl-tRNA to sense nascent chain occupancy. Structural and mutational analyses showed that ribosome-bound NEMF recruits and stabilizes Listerin's N-terminal domain, while Listerin's C-terminal RWD domain directly contacts the ribosome to position the adjacent ligase domain near the nascent polypeptide exit tunnel. Thus, highly specific nascent chain targeting by Listerin is imparted by the avidity gained from a multivalent network of context-specific individually weak interactions, highlighting a new principle of client recognition during protein quality control.
Structure and Assembly Pathway of the Ribosome Quality Control Complex.,Shao S, Brown A, Santhanam B, Hegde RS Mol Cell. 2015 Jan 7. pii: S1097-2765(14)00964-2. doi:, 10.1016/j.molcel.2014.12.015. PMID:25578875[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
↑ Bi X, Jones T, Abbasi F, Lee H, Stultz B, Hursh DA, Mortin MA. Drosophila caliban, a nuclear export mediator, can function as a tumor suppressor in human lung cancer cells. Oncogene. 2005 Dec 15;24(56):8229-39. PMID:16103875 doi:http://dx.doi.org/10.1038/sj.onc.1208962
↑ Shao S, Brown A, Santhanam B, Hegde RS. Structure and Assembly Pathway of the Ribosome Quality Control Complex. Mol Cell. 2015 Jan 7. pii: S1097-2765(14)00964-2. doi:, 10.1016/j.molcel.2014.12.015. PMID:25578875 doi:http://dx.doi.org/10.1016/j.molcel.2014.12.015
