3j7r

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{{Large structure}}
==Structure of the translating mammalian ribosome-Sec61 complex==
==Structure of the translating mammalian ribosome-Sec61 complex==
<StructureSection load='3j7r' size='340' side='right' caption='[[3j7r]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
<StructureSection load='3j7r' size='340' side='right' caption='[[3j7r]], [[Resolution|resolution]] 3.90&Aring;' scene=''>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNK:UNKNOWN'>UNK</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j7o|3j7o]], [[3j7p|3j7p]], [[3j7q|3j7q]]</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3j7o|3j7o]], [[3j7p|3j7p]], [[3j7q|3j7q]]</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j7r OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3j7r RCSB], [http://www.ebi.ac.uk/pdbsum/3j7r PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3j7r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3j7r OCA], [http://pdbe.org/3j7r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3j7r RCSB], [http://www.ebi.ac.uk/pdbsum/3j7r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3j7r ProSAT]</span></td></tr>
</table>
</table>
{{Large structure}}
{{Large structure}}
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/RS18_PIG RS18_PIG]] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity). [[http://www.uniprot.org/uniprot/RL40_PIG RL40_PIG]] Ubiquitin: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). 60S ribosomal protein L40: component of the 60S subunit of the ribosome (By similarity). [[http://www.uniprot.org/uniprot/B6V8C8_PIG B6V8C8_PIG]] May play a role during erythropoiesis through regulation of transcription factor DDIT3 (By similarity).[HAMAP-Rule:MF_03122] [[http://www.uniprot.org/uniprot/RL11_PIG RL11_PIG]] Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML (By similarity). [[http://www.uniprot.org/uniprot/RSSA_PIG RSSA_PIG]] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA (By similarity).<ref>PMID:15790424</ref>
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[[http://www.uniprot.org/uniprot/RL40_PIG RL40_PIG]] Ubiquitin: exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity). 60S ribosomal protein L40: component of the 60S subunit of the ribosome (By similarity). [[http://www.uniprot.org/uniprot/B6V8C8_PIG B6V8C8_PIG]] May play a role during erythropoiesis through regulation of transcription factor DDIT3 (By similarity).[HAMAP-Rule:MF_03122] [[http://www.uniprot.org/uniprot/RS18_PIG RS18_PIG]] Located at the top of the head of the 40S subunit, it contacts several helices of the 18S rRNA (By similarity). [[http://www.uniprot.org/uniprot/RL11_PIG RL11_PIG]] Binds to 5S ribosomal RNA (By similarity). Required for rRNA maturation and formation of the 60S ribosomal subunits. Promotes nucleolar location of PML (By similarity). [[http://www.uniprot.org/uniprot/RSSA_PIG RSSA_PIG]] Required for the assembly and/or stability of the 40S ribosomal subunit. Required for the processing of the 20S rRNA-precursor to mature 18S rRNA in a late step of the maturation of 40S ribosomal subunits. Also functions as a cell surface receptor for laminin. Plays a role in cell adhesion to the basement membrane and in the consequent activation of signaling transduction pathways. May play a role in cell fate determination and tissue morphogenesis. Also acts as a receptor for several other ligands, including the pathogenic prion protein, viruses, and bacteria. Acts as a PPP1R16B-dependent substrate of PPP1CA (By similarity).<ref>PMID:15790424</ref>
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<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3j7r" style="background-color:#fffaf0;"></div>
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==See Also==
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*[[TRNA|TRNA]]
== References ==
== References ==
<references/>
<references/>

Revision as of 08:16, 18 July 2018

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Structure of the translating mammalian ribosome-Sec61 complex

3j7r, resolution 3.90Å

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