5yks: Difference between revisions
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==Crystal structure of sucrose nonfermenting-related kinase (SNRK)== | |||
<StructureSection load='5yks' size='340' side='right'caption='[[5yks]], [[Resolution|resolution]] 2.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5yks]] is a 2 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=5YKS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YKS FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</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=5yks FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5yks OCA], [https://pdbe.org/5yks PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5yks RCSB], [https://www.ebi.ac.uk/pdbsum/5yks PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5yks ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/SNRK_HUMAN SNRK_HUMAN] May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis.[UniProtKB:Q63553]<ref>PMID:12234663</ref> <ref>PMID:15733851</ref> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Sucrose non-fermenting (Snf1)-related kinase (SNRK) is a novel member of the AMP-activated protein kinase (AMPK) family and is involved in many metabolic processes. Here we report the crystal structure of an N-terminal SNRK fragment containing kinase and adjacent ubiquitin-associated (UBA) domains. This structure shows that the UBA domain binds between the N- and C-lobes of the kinase domain. The mode of UBA binding in SNRK largely resembles that in AMPK and brain specific kinase (BRSK), however, unique interactions play vital roles in stabilizing the KD-UBA interface of SNRK. We further propose a potential role of the UBA domain in the regulation of SNRK kinase activity. This study provides new insights into the structural diversities of the AMPK kinase family. | |||
Crystal structure of the kinase and UBA domains of SNRK reveals a distinct UBA binding mode in the AMPK family.,Wang YL, Wang J, Chen X, Wang ZX, Wu JW Biochem Biophys Res Commun. 2017 Oct 20. pii: S0006-291X(17)32083-1. doi:, 10.1016/j.bbrc.2017.10.105. PMID:29061304<ref>PMID:29061304</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5yks" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Serine/threonine protein kinase 3D structures|Serine/threonine protein kinase 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | |||
[[Category: Wang J]] | |||
[[Category: Wang YL]] | |||
[[Category: Wu JW]] | |||
Latest revision as of 11:32, 22 November 2023
Structural highlights
FunctionSNRK_HUMAN May play a role in hematopoietic cell proliferation or differentiation. Potential mediator of neuronal apoptosis.[UniProtKB:Q63553][1] [2] Publication Abstract from PubMedSucrose non-fermenting (Snf1)-related kinase (SNRK) is a novel member of the AMP-activated protein kinase (AMPK) family and is involved in many metabolic processes. Here we report the crystal structure of an N-terminal SNRK fragment containing kinase and adjacent ubiquitin-associated (UBA) domains. This structure shows that the UBA domain binds between the N- and C-lobes of the kinase domain. The mode of UBA binding in SNRK largely resembles that in AMPK and brain specific kinase (BRSK), however, unique interactions play vital roles in stabilizing the KD-UBA interface of SNRK. We further propose a potential role of the UBA domain in the regulation of SNRK kinase activity. This study provides new insights into the structural diversities of the AMPK kinase family. Crystal structure of the kinase and UBA domains of SNRK reveals a distinct UBA binding mode in the AMPK family.,Wang YL, Wang J, Chen X, Wang ZX, Wu JW Biochem Biophys Res Commun. 2017 Oct 20. pii: S0006-291X(17)32083-1. doi:, 10.1016/j.bbrc.2017.10.105. PMID:29061304[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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