Ribosomal protein L29

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<StructureSection load='' size='350' side='right' caption='Ribosomal protein L29 NMR structure, (PDB code [[1r73]])' scene='Ribosomal_protein_L29/Cv/1'>
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{{STRUCTURE_1r73| PDB=1r73 | SIZE=300| SCENE=Ribosomal_protein_L29/Cv/1 |right|CAPTION=Ribosomal protein L29 NMR structure ([[1r73]]) }}
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'''Ribosomal protein L29''' (RPL29) is one of the 34 proteins which belong to the large 50S subunit of the prokaryotic ribosome or to the ca. 49 proteins in the large 60S subunit of the eukaryotic ribosome. RPL29 binds heparin and as such has a secondary function besides protein biosynthesis.
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'''Ribosomal protein L29''' (RPL29) is one of the 34 proteins which belong to the large 50S subunit of the prokaryotic ribosome or to the ca. 49 proteins in the large 60S subunit of the eukaryotic ribosome<ref>PMID:23118343</ref>. RPL29 binds heparin and as such has a secondary function besides protein biosynthesis.
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</StructureSection>
== 3D Structures of Ribosomal protein L29 ==
== 3D Structures of Ribosomal protein L29 ==
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**[[1r73]] – RPL29 – ''Thermotoga maritime'' - NMR
**[[1r73]] – RPL29 – ''Thermotoga maritime'' - NMR
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*Ribosomal protein L25 in part of the 50S subunit
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*Ribosomal protein L29 in part of the 50S subunit
**[[2vrh]] – EcRPL29 + RPL23 + RPL24 + trigger factor - ''Escherichia coli''<br />
**[[2vrh]] – EcRPL29 + RPL23 + RPL24 + trigger factor - ''Escherichia coli''<br />
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**[[2aar]] - DrRPL29 + RPL23 + 23S RRNA + trigger factor - ''Deinococcus radiodurans''<br />
**[[2aar]] - DrRPL29 + RPL23 + 23S RRNA + trigger factor - ''Deinococcus radiodurans''<br />
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}}
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== References ==
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<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Ribosomal protein L29 NMR structure, (PDB code 1r73)

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3D Structures of Ribosomal protein L29

Updated on 29-September-2017

References

  1. Jones DT, Lechertier T, Reynolds LE, Mitter R, Robinson SD, Kirn-Safran CB, Hodivala-Dilke KM. Endogenous ribosomal protein L29 (RPL29): a newly identified regulator of angiogenesis in mice. Dis Model Mech. 2013 Jan;6(1):115-24. doi: 10.1242/dmm.009183. Epub 2012 Nov 1. PMID:23118343 doi:http://dx.doi.org/10.1242/dmm.009183

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