Proto-oncogene serine/threonine-protein kinase
From Proteopedia
(Difference between revisions)
| Line 17: | Line 17: | ||
[[3D structures of pim-1]] | [[3D structures of pim-1]] | ||
</StructureSection> | </StructureSection> | ||
| - | == 3D Structures of pim-1 == | ||
| - | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| - | |||
| - | *Pim1; Domains catalytic 14-313; kinase 92-404 | ||
| - | |||
| - | **[[1xqz]], [[1ywv]], [[4jx3]] – hPim1 catalytic domain 14-313 – human <br /> | ||
| - | **[[1yxs]] – hPim1 catalytic domain (mutant) <br /> | ||
| - | **[[4jx3]] – hPim1 kinase domain residues 92-404 <br /> | ||
| - | **[[1xr1]], [[1yxt]] – hPim1 catalytic domain + AMPPNP <br /> | ||
| - | **[[1yxu]] – hPim1 catalytic domain + AMP <br /> | ||
| - | **[[1yxv]] – hPim1 catalytic domain + quinoline derivative <br /> | ||
| - | **[[3uix]] – hPim1 kinase domain residues 120-404 + quinoline derivative <br /> | ||
| - | **[[1yxx]] – hPim1 catalytic domain + indole derivative <br /> | ||
| - | **[[3a99]] – hPim1 kinase domain + phosphoaminophosphonic acid adenylate <br /> | ||
| - | **[[2bzj]], [[2bzh]], [[2bzi]] – hPim1 catalytic domain (mutant) + organometallic ligand <br /> | ||
| - | **[[2oi4]], [[3bwf]] – hPim1 kinase domain (mutant) + organometallic ligand <br /> | ||
| - | **[[1xws]], [[4dtk]], [[4as0]], [[4alu]], [[4alv]], [[4alw]], [[4bzn]], [[4bzo]], [[6bsk]], [[5v80]], [[5toe]], [[5tex]], [[5tel]], [[5o11]], [[5o12]], [[5o13]] – hPim1 kinase domain + inhibitor <br /> | ||
| - | **[[6ayd]] – hPim1 kinase domain (mutant)+ inhibitor <br /> | ||
| - | **[[2o3p]], [[2o63]], [[2o64]], [[2o65]], [[3jxw]], [[3jy0]], [[3jya]], [[3r00]], [[3r01]], [[3r02]], [[3r04]], [[3vbq]], [[3vbt]], [[3vbv]], [[3vbw]], [[3vbx]], [[3vby]], [[3vc4]], [[3umx]], [[4enx]], [[4eny]], [[3umw]], [[4ll5]], [[4lm5]], [[3c4e]], [[5vuc]], [[5vub]], [[5vua]], [[4n70]], [[4n6z]], [[4n6y]], [[4mta]], [[4med]], [[4mbl]], [[4mbi]], [[4lmu]], [[4k1b]], [[4k18]], [[4k0y]], [[4iaa]], [[4i41]], [[6mt0]] – hPim1 catalytic domain + inhibitor <br /> | ||
| - | **[[2j2i]], [[3we8]] – hPim1 catalytic domain (mutant)+ inhibitor <br /> | ||
| - | **[[5tur]] - hPim1 + inhibitor <br /> | ||
| - | |||
| - | *Pim1 complex with consensus peptide | ||
| - | |||
| - | **[[2bil]], [[3cxw]], [[3cy2]], [[3cy3]], [[6qxk]], [[6pcw]], [[6pdi]], [[6pdn]], [[6pdo]], [[6pdp]] – hPim1 kinase domain + inhibitor + consensus peptide<br /> | ||
| - | **[[3jpv]], [[3qf9]] - hPim1 catalytic domain + inhibitor + consensus peptide<br /> | ||
| - | **[[2c3i]], [[5ndt]], [[5n5m]], [[5n5l]], [[5n52]], [[5n51]], [[5n50]], [[5n4z]], [[5n4y]], [[5n4x]], [[5n4v]], [[5n4u]], [[5n4r]], [[5n4o]], [[5n4n]], [[5mzl]] – hPim1 kinase domain (mutant) + inhibitor + consensus peptide <br /> | ||
| - | **[[4gw8]] – hPim1 catalytic domain (mutant) + inhibitor + consensus peptide <br /> | ||
| - | **[[2bzk]] – hPim1 kinase domain (mutant)+ AMPPNP + consensus peptide <br /> | ||
| - | **[[3ma3]] – hPim1 catalytic domain + inhibitor + PSer + consensus peptide<br /> | ||
| - | |||
| - | *Pim1 containing phosphorylated Ser 261 | ||
| - | |||
| - | **[[1yhs]] – hPim1 kinase domain + PSer + staurosporine <br /> | ||
| - | **[[1yi3]], [[2bik]], [[2xix]], [[2xiy]], [[2xiz]], [[2xj0]], [[2xj1]], [[2xj2]], [[4a7c]] – hPim1 kinase domain + PSer + inhibitor <br /> | ||
| - | **[[2obj]], [[3bgp]], [[3bgq]], [[3bgz]], [[3dcv]], [[3f2a]], [[3t9i]] - hPim1 catalytic domain + PSer + inhibitor <br /> | ||
| - | **[[1yi4]] – hPim1 kinase domain + PSer + adenosine <br /> | ||
| - | |||
| - | *Pim1 raf see [[Serine/threonine protein kinase]] | ||
| - | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 10:13, 19 October 2020
| |||||||||||
References
- ↑ Bachmann M, Moroy T. The serine/threonine kinase Pim-1. Int J Biochem Cell Biol. 2005 Apr;37(4):726-30. PMID:15694833 doi:http://dx.doi.org/10.1016/j.biocel.2004.11.005
- ↑ Brault L, Menter T, Obermann EC, Knapp S, Thommen S, Schwaller J, Tzankov A. PIM kinases are progression markers and emerging therapeutic targets in diffuse large B-cell lymphoma. Br J Cancer. 2012 Jul 24;107(3):491-500. doi: 10.1038/bjc.2012.272. Epub 2012 Jun, 21. PMID:22722314 doi:http://dx.doi.org/10.1038/bjc.2012.272
- ↑ Weirauch U, Beckmann N, Thomas M, Grunweller A, Huber K, Bracher F, Hartmann RK, Aigner A. Functional role and therapeutic potential of the pim-1 kinase in colon carcinoma. Neoplasia. 2013 Jul;15(7):783-94. PMID:23814490
- ↑ Huber K, Brault L, Fedorov O, Gasser C, Filippakopoulos P, Bullock AN, Fabbro D, Trappe J, Schwaller J, Knapp S, Bracher F. 7,8-Dichloro-1-oxo-beta-carbolines as a Versatile Scaffold for the Development of Potent and Selective Kinase Inhibitors with Unusual Binding Modes. J Med Chem. 2012 Jan 12;55(1):403-13. Epub 2012 Jan 3. PMID:22136433 doi:10.1021/jm201286z

