| Structural highlights5opt is a 35 chain structure with sequence from Trycc. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
| Gene: | Tc00.1047053511211.120, Tc00.1047053511211.130 (TRYCC), Tc00.1047053511291.90 (TRYCC), Tc00.1047053506963.14, Tc00.1047053511233.14, Tc00.1047053511277.175 (TRYCC), Tc00.1047053503801.20, Tc00.1047053508817.60 (TRYCC), Tc00.1047053511237.60 (TRYCC), Tc00.1047053409117.20, Tc00.1047053506945.230, Tc00.1047053508823.50 (TRYCC), Tc00.1047053511001.9, Tc00.1047053511001.18 (TRYCC), Tc00.1047053508319.70, Tc00.1047053508405.40 (TRYCC), Tc00.1047053507681.150, Tc00.1047053507681.160 (TRYCC), Tc00.1047053511903.110 (TRYCC), Tc00.1047053504163.30, Tc00.1047053506401.120 (TRYCC), Tc00.1047053506025.14, Tc00.1047053511209.54, Tc00.1047053511805.15 (TRYCC), Tc00.1047053510425.19 (TRYCC), Tc00.1047053503833.40, Tc00.1047053506213.60, Tc00.1047053511287.120, Tc00.1047053511287.40 (TRYCC), Tc00.1047053506297.330 (TRYCC), Tc00.1047053510101.420 (TRYCC), Tc00.1047053504105.94, Tc00.1047053509233.190 (TRYCC), Tc00.1047053503395.50, Tc00.1047053506181.59 (TRYCC), Tc00.1047053510409.39 (TRYCC), Tc00.1047053510769.49 (TRYCC), Tc00.1047053508827.70 (TRYCC), Tc00.1047053508475.10, Tc00.1047053508823.120, Tc00.1047053508823.140 (TRYCC), Tc00.1047053503899.20, Tc00.1047053503899.30 (TRYCC), Tc00.1047053504021.109, Tc00.1047053507677.39, Tc00.1047053509353.30 (TRYCC), Tc00.1047053506679.140, Tc00.1047053506679.150 (TRYCC), Tc00.1047053510879.20 (TRYCC), Tc00.1047053507019.83, Tc00.1047053507019.86 (TRYCC), Tc00.1047053511727.270 (TRYCC), Tc00.1047053511809.130, Tc00.1047053511809.99, Tc00.1047053511811.10 (TRYCC), Tc00.1047053506679.100, Tc00.1047053506679.94 (TRYCC), Tc00.1047053509683.117, Tc00.1047053511051.39, Tc00.1047053511051.50 (TRYCC), Tc00.1047053504181.20, Tc00.1047053504181.30, Tc00.1047053509695.180, Tc00.1047053509695.184 (TRYCC), Tc00.1047053506297.150, Tc00.1047053506297.160 (TRYCC), Tc00.1047053506593.30 (TRYCC) |
Experimental data: | Check | Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function[Q4CQ63_TRYCC] 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.[HAMAP-Rule:MF_03015]
Publication Abstract from PubMed
Kinetoplastids are potentially lethal protozoan pathogens affecting more than 20 million people worldwide. There is a critical need for more specific targets for the development of safer anti-kinetoplastid therapeutic molecules that can replace the scarce and highly cytotoxic current drugs. The kinetoplastid ribosome represents a potential therapeutic target due to its relative structural divergence when compared with its human counterpart. However, several kinetoplastid-specific ribosomal features remain uncharacterized. Here, we present the near-atomic cryoelectron microscopy structure of a novel bona fide kinetoplastid-specific ribosomal (r-) protein (KSRP) bound to the ribosome. KSRP is an essential protein located at the solvent face of the 40S subunit, where it binds and stabilizes kinetoplastid-specific domains of rRNA, suggesting its role in ribosome integrity. KSRP also interacts with the r-protein eS6 at a region that is only conserved in kinetoplastids. The kinetoplastid-specific ribosomal environment of KSRP provides a promising target for the design of safer anti-kinetoplastidian drugs.
The cryo-EM Structure of a Novel 40S Kinetoplastid-Specific Ribosomal Protein.,Brito Querido J, Mancera-Martinez E, Vicens Q, Bochler A, Chicher J, Simonetti A, Hashem Y Structure. 2017 Oct 13. pii: S0969-2126(17)30305-2. doi:, 10.1016/j.str.2017.09.014. PMID:29107485[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See AlsoReferences
- ↑ Brito Querido J, Mancera-Martinez E, Vicens Q, Bochler A, Chicher J, Simonetti A, Hashem Y. The cryo-EM Structure of a Novel 40S Kinetoplastid-Specific Ribosomal Protein. Structure. 2017 Oct 13. pii: S0969-2126(17)30305-2. doi:, 10.1016/j.str.2017.09.014. PMID:29107485 doi:http://dx.doi.org/10.1016/j.str.2017.09.014
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