Protein patched homolog 1
From Proteopedia
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
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| + | Domains: ectodomain 1 139-428; ectodomain 2 772-1023 | ||
[[6dmb]], [[6oeu]] – hPtch1 – human - Cryo EM <br /> | [[6dmb]], [[6oeu]] – hPtch1 – human - Cryo EM <br /> | ||
[[6dmo]] – hPtch1 (mutant) - Cryo EM <br /> | [[6dmo]] – hPtch1 (mutant) - Cryo EM <br /> | ||
| - | [[6rtx]] – hPtch1 ectodomain 1 | + | [[6rvd]] – hPtch1 + sonic hedgehog protein - Cryo EM <br /> |
| + | [[6dmy]], [[6e1h]], [[6n7g]], [[6n7h]], [[6n7k]], [[6oev]], [[6rmg]] – hPtch1/GFP + sonic hedgehog protein - Cryo EM <br /> | ||
| + | [[6rtx]] – hPtch1 ectodomain 1<br /> | ||
[[6rty]] – hPtch1 ectodomain 1 + nanobody <br /> | [[6rty]] – hPtch1 ectodomain 1 + nanobody <br /> | ||
| - | [[6rvc]] – hPtch1 ectodomain 2 772-1023 + nanobody <br /> | ||
[[6rtw]] – hPtch1 ectodomain 1 + nanobody + cholesterol derivative <br /> | [[6rtw]] – hPtch1 ectodomain 1 + nanobody + cholesterol derivative <br /> | ||
| + | [[6rvc]] – hPtch1 ectodomain 2 + nanobody <br /> | ||
[[6mg8]] – Ptch1 + ligand – mouse - Cryo EM <br /> | [[6mg8]] – Ptch1 + ligand – mouse - Cryo EM <br /> | ||
Revision as of 09:14, 6 February 2021
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3D Structures of protein patched homolog 1
Updated on 06-February-2021
Domains: ectodomain 1 139-428; ectodomain 2 772-1023
6dmb, 6oeu – hPtch1 – human - Cryo EM
6dmo – hPtch1 (mutant) - Cryo EM
6rvd – hPtch1 + sonic hedgehog protein - Cryo EM
6dmy, 6e1h, 6n7g, 6n7h, 6n7k, 6oev, 6rmg – hPtch1/GFP + sonic hedgehog protein - Cryo EM
6rtx – hPtch1 ectodomain 1
6rty – hPtch1 ectodomain 1 + nanobody
6rtw – hPtch1 ectodomain 1 + nanobody + cholesterol derivative
6rvc – hPtch1 ectodomain 2 + nanobody
6mg8 – Ptch1 + ligand – mouse - Cryo EM
References
- ↑ Wolff EC, Park MH, Folk JE. Cleavage of spermidine as the first step in deoxyhypusine synthesis. The role of NAD. J Biol Chem. 1990 Mar 25;265(9):4793-9. PMID:2108161
- ↑ Ganapathi M, Padgett LR, Yamada K, Devinsky O, Willaert R, Person R, Au PB, Tagoe J, McDonald M, Karlowicz D, Wolf B, Lee J, Shen Y, Okur V, Deng L, LeDuc CA, Wang J, Hanner A, Mirmira RG, Park MH, Mastracci TL, Chung WK. Recessive Rare Variants in Deoxyhypusine Synthase, an Enzyme Involved in the Synthesis of Hypusine, Are Associated with a Neurodevelopmental Disorder. Am J Hum Genet. 2019 Feb 7;104(2):287-298. doi: 10.1016/j.ajhg.2018.12.017. Epub , 2019 Jan 17. PMID:30661771 doi:http://dx.doi.org/10.1016/j.ajhg.2018.12.017
- ↑ Colvin SC, Maier B, Morris DL, Tersey SA, Mirmira RG. Deoxyhypusine synthase promotes differentiation and proliferation of T helper type 1 (Th1) cells in autoimmune diabetes. J Biol Chem. 2013 Dec 20;288(51):36226-35. doi: 10.1074/jbc.M113.473942. Epub, 2013 Nov 6. PMID:24196968 doi:http://dx.doi.org/10.1074/jbc.M113.473942
- ↑ Wator E, Wilk P, Grudnik P. Half Way to Hypusine-Structural Basis for Substrate Recognition by Human Deoxyhypusine Synthase. Biomolecules. 2020 Mar 30;10(4). pii: biom10040522. doi: 10.3390/biom10040522. PMID:32235505 doi:http://dx.doi.org/10.3390/biom10040522
