2zv2
From Proteopedia
Contents |
Crystal structure of human calcium/calmodulin-dependent protein kinase kinase 2, beta, CaMKK2 kinase domain in complex with STO-609
Template:ABSTRACT PUBMED 21504895
Function
[KKCC2_HUMAN] Calcium/calmodulin-dependent protein kinase belonging to a proposed calcium-triggered signaling cascade involved in a number of cellular processes. Isoform 1, isoform 2 and isoform 3 phosphorylate CAMK1 and CAMK4. Isoform 3 phosphorylates CAMK1D. Isoform 4, isoform 5 and isoform 6 lacking part of the calmodulin-binding domain are inactive. Efficiently phosphorylates 5'-AMP-activated protein kinase (AMPK) trimer, including that consisting of PRKAA1, PRKAB1 and PRKAG1. This phosphorylation is stimulated in response to Ca(2+) signals (By similarity). Seems to be involved in hippocampal activation of CREB1 (By similarity). May play a role in neurite growth. Isoform 3 may promote neurite elongation, while isoform 1 may promoter neurite branching.[1] [2] [3] [4]
About this Structure
2zv2 is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA.
Reference
- Kukimoto-Niino M, Yoshikawa S, Takagi T, Ohsawa N, Tomabechi Y, Terada T, Shirouzu M, Suzuki A, Lee S, Yamauchi T, Okada-Iwabu M, Iwabu M, Kadowaki T, Minokoshi Y, Yokoyama S. Crystal structure of the CA2+/calmodulin-dependent protein kinase kinase in complex with the inhibitor STO-609. J Biol Chem. 2011 Apr 19. PMID:21504895 doi:10.1074/jbc.M111.251710
- ↑ Hsu LS, Chen GD, Lee LS, Chi CW, Cheng JF, Chen JY. Human Ca2+/calmodulin-dependent protein kinase kinase beta gene encodes multiple isoforms that display distinct kinase activity. J Biol Chem. 2001 Aug 17;276(33):31113-23. Epub 2001 Jun 6. PMID:11395482 doi:http://dx.doi.org/10.1074/jbc.M011720200
- ↑ Ishikawa Y, Tokumitsu H, Inuzuka H, Murata-Hori M, Hosoya H, Kobayashi R. Identification and characterization of novel components of a Ca2+/calmodulin-dependent protein kinase cascade in HeLa cells. FEBS Lett. 2003 Aug 28;550(1-3):57-63. PMID:12935886
- ↑ Hsu LS, Tsou AP, Chi CW, Lee CH, Chen JY. Cloning, expression and chromosomal localization of human Ca2+/calmodulin-dependent protein kinase kinase. J Biomed Sci. 1998;5(2):141-9. PMID:9662074
- ↑ Cao W, Sohail M, Liu G, Koumbadinga GA, Lobo VG, Xie J. Differential effects of PKA-controlled CaMKK2 variants on neuronal differentiation. RNA Biol. 2011 Nov-Dec;8(6):1061-72. doi: 10.4161/rna.8.6.16691. Epub 2011 Nov 1. PMID:21957496 doi:http://dx.doi.org/10.4161/rna.8.6.16691
Categories: Calcium/calmodulin-dependent protein kinase | Human | Kukimoto-niino, M. | Lee, S. | Minokoshi, Y. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Shirouzu, M. | Suzuki, A. | Yokoyama, S. | Yoshikawa, S. | Ampkk | Atp-binding | Beta | Calcium/calmodulin-dependent protein kinase kinase 2 | Calmodulin-binding | Camkk2 | E c.2 7.11 17 | Kinase | Metabolism | National project on protein structural and functional analyse | Nppsfa | Nucleotide-binding | Phosphoprotein | Phosphorylation | Riken structural genomics/proteomics initiative | Rsgi | Serine/threonine-protein kinase | Sto-609 | Structural genomic | Transferase | Transferase-transferase inhibitor complex
