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==Crystal Structure of BMP-2-inducible kinase in complex with baricitinib== | ==Crystal Structure of BMP-2-inducible kinase in complex with baricitinib== | ||
<StructureSection load='4w9x' size='340' side='right' caption='[[4w9x]], [[Resolution|resolution]] 2.14Å' scene=''> | <StructureSection load='4w9x' size='340' side='right'caption='[[4w9x]], [[Resolution|resolution]] 2.14Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4w9x]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W9X OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[4w9x]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4W9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4W9X FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.14Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3JW:BARICITINIB'>3JW</scene>, <scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4w9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4w9x OCA], [https://pdbe.org/4w9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4w9x RCSB], [https://www.ebi.ac.uk/pdbsum/4w9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4w9x ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/BMP2K_HUMAN BMP2K_HUMAN] May be involved in osteoblast differentiation. | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The highly diverse Numb-associated kinase (NAK) family has been linked to broad cellular functions including receptor-mediated endocytosis, Notch pathway modulation, osteoblast differentiation, and dendrite morphogenesis. Consequently, NAK kinases play a key role in a diverse range of diseases from Parkinson's and prostate cancer to HIV. Due to the plasticity of this kinase family, NAK kinases are often inhibited by approved or investigational drugs and have been associated with side effects, but they are also potential drug targets. The presence of cysteine residues in some NAK family members provides the possibility for selective targeting via covalent inhibition. Here we report the first high-resolution structures of kinases AAK1 and BIKE in complex with two drug candidates. The presented data allow a comprehensive structural characterization of the NAK kinase family and provide the basis for rational design of selective NAK inhibitors. | |||
Family-wide Structural Analysis of Human Numb-Associated Protein Kinases.,Sorrell FJ, Szklarz M, Abdul Azeez KR, Elkins JM, Knapp S Structure. 2016 Jan 29. pii: S0969-2126(16)00008-3. doi:, 10.1016/j.str.2015.12.015. PMID:26853940<ref>PMID:26853940</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4w9x" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: | [[Category: Arrowsmith CH]] | ||
[[Category: | [[Category: Bountra C]] | ||
[[Category: Edwards | [[Category: Edwards AM]] | ||
[[Category: Elkins | [[Category: Elkins JM]] | ||
[[Category: Knapp | [[Category: Knapp S]] | ||
[[Category: Krojer | [[Category: Krojer T]] | ||
[[Category: Savitsky P]] | |||
[[Category: Savitsky | [[Category: Sorrell FJ]] | ||
[[Category: Sorrell | [[Category: Williams E]] | ||
[[Category: Williams | [[Category: Von Delft F]] | ||
[[Category: | |||
Latest revision as of 14:27, 9 May 2024
Crystal Structure of BMP-2-inducible kinase in complex with baricitinibCrystal Structure of BMP-2-inducible kinase in complex with baricitinib
Structural highlights
FunctionBMP2K_HUMAN May be involved in osteoblast differentiation. Publication Abstract from PubMedThe highly diverse Numb-associated kinase (NAK) family has been linked to broad cellular functions including receptor-mediated endocytosis, Notch pathway modulation, osteoblast differentiation, and dendrite morphogenesis. Consequently, NAK kinases play a key role in a diverse range of diseases from Parkinson's and prostate cancer to HIV. Due to the plasticity of this kinase family, NAK kinases are often inhibited by approved or investigational drugs and have been associated with side effects, but they are also potential drug targets. The presence of cysteine residues in some NAK family members provides the possibility for selective targeting via covalent inhibition. Here we report the first high-resolution structures of kinases AAK1 and BIKE in complex with two drug candidates. The presented data allow a comprehensive structural characterization of the NAK kinase family and provide the basis for rational design of selective NAK inhibitors. Family-wide Structural Analysis of Human Numb-Associated Protein Kinases.,Sorrell FJ, Szklarz M, Abdul Azeez KR, Elkins JM, Knapp S Structure. 2016 Jan 29. pii: S0969-2126(16)00008-3. doi:, 10.1016/j.str.2015.12.015. PMID:26853940[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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