Increased sodium tolerance protein

(Difference between revisions)

Revision as of 08:13, 19 May 2020

Yeast Ist1 N-terminal (grey) complex with ESCRT-III subunit Did2 (pink) (PDB code 3ggz)

Drag the structure with the mouse to rotate

Updated on 19-May-2020

↑ Bajorek M, Schubert HL, McCullough J, Langelier C, Eckert DM, Stubblefield WM, Uter NT, Myszka DG, Hill CP, Sundquist WI. Structural basis for ESCRT-III protein autoinhibition. Nat Struct Mol Biol. 2009 Jul;16(7):754-62. Epub 2009 Jun 14. PMID:19525971 doi:10.1038/nsmb.1621
↑ Fong YW, Zhou Q. Stimulatory effect of splicing factors on transcriptional elongation. Nature. 2001 Dec 20-27;414(6866):929-33. PMID:11780068 doi:http://dx.doi.org/10.1038/414929a
↑ Tanikawa M, Sanjiv K, Helleday T, Herr P, Mortusewicz O. The spliceosome U2 snRNP factors promote genome stability through distinct mechanisms; transcription of repair factors and R-loop processing. Oncogenesis. 2016 Dec 19;5(12):e280. doi: 10.1038/oncsis.2016.70. PMID:27991914 doi:http://dx.doi.org/10.1038/oncsis.2016.70
↑ Xiao J, Chen XW, Davies BA, Saltiel AR, Katzmann DJ, Xu Z. Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis. Mol Biol Cell. 2009 Aug;20(15):3514-24. Epub 2009 May 28. PMID:19477918 doi:10.1091/mbc.E09-05-0403

@@ Line 8: / Line 8: @@
 == Disease ==
-Somatic mutations in Ist3 have been found in various malignancies like breast cancer, pancreatuc cancer, uveal melanoma and others<ref>PMID:27991914</ref>.
+Somatic mutations in Ist3 have been found in various malignancies like breast cancer, pancreatic cancer, uveal melanoma and others<ref>PMID:27991914</ref>.
-== Relevance ==
 == Structural highlights ==
-The structure of the yeast Ist1 N-terminal complex with ESCRT-III subunit Did2 which is part of a high-order helical structure shows. Six side chains of Ist1 point toward the Did2 helix but only 3 of those were found by mutational studies to interact with 5 Did2 side chains<ref>PMID:19477918</ref>.
+The structure of the yeast Ist1 N-terminal complex with ESCRT-III subunit Did2 which is part of a high-order helical structure shows six side chains of Ist1 pointing toward the Did2 helix. Only 3 of those were found by mutational studies to interact with 5 side chains of Did2<ref>PMID:19477918</ref>.