Ribosomal protein S17
From Proteopedia
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<StructureSection load='2zm6' size='350' side='right' caption='Ribosomal protein S17 from [[2zm6]], chain Q' scene='Ribosomal_protein_S17/Cv/1'> | <StructureSection load='2zm6' size='350' side='right' caption='Ribosomal protein S17 from [[2zm6]], chain Q' scene='Ribosomal_protein_S17/Cv/1'> | ||
| + | == Function == | ||
'''Ribosomal protein S17''' (RPS17) is one of the 21 proteins which belong to the 30S <scene name='Ribosomal_protein_S17/Cv/2'>small subunit</scene> of the [http://en.wikipedia.org/wiki/Bacteria bacterial] [[ribosome]] or the 30 proteins which belong to the 40S small subunit of the eukaryotic ribosome. It binds to the 5' end of 16S RRNA and may participate in the recognition of termination codons. | '''Ribosomal protein S17''' (RPS17) is one of the 21 proteins which belong to the 30S <scene name='Ribosomal_protein_S17/Cv/2'>small subunit</scene> of the [http://en.wikipedia.org/wiki/Bacteria bacterial] [[ribosome]] or the 30 proteins which belong to the 40S small subunit of the eukaryotic ribosome. It binds to the 5' end of 16S RRNA and may participate in the recognition of termination codons. | ||
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| + | == Disease == | ||
| + | RPS17 mutations are present in patients with Diamond-Blackfan anemia<ref>PMID:17647292</ref>. | ||
</StructureSection> | </StructureSection> | ||
== 3D Structures of Ribosomal protein S17 == | == 3D Structures of Ribosomal protein S17 == | ||
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**[[1qd7]] - TtRPS17+TtRPS4+TtRPS5+TtRPS7+TtRPS8+TtRPS6+TtRPS15+TtRPS20+16S RRNA fragment - ''Thermus thermophilus''<br /> | **[[1qd7]] - TtRPS17+TtRPS4+TtRPS5+TtRPS7+TtRPS8+TtRPS6+TtRPS15+TtRPS20+16S RRNA fragment - ''Thermus thermophilus''<br /> | ||
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| - | + | == References == | |
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[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Current revision
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3D Structures of Ribosomal protein S17
Updated on 16-August-2016
References
- ↑ Cmejla R, Cmejlova J, Handrkova H, Petrak J, Pospisilova D. Ribosomal protein S17 gene (RPS17) is mutated in Diamond-Blackfan anemia. Hum Mutat. 2007 Dec;28(12):1178-82. PMID:17647292 doi:10.1002/humu.20608
