5L2Q

Serine/threonine-protein kinase 40 (STK40) kinase homology domain

Summary for 5L2Q

• Entry DOI: 10.2210/pdb5l2q/pdb
• Descriptor: Serine/threonine-protein kinase 40 (2 entities in total)
• Functional Keywords: pseudokinase sink-homologous serine/threonine-protein kinase sugen kinase 495, transferase
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 4
• Total formula weight: 144602.53

Authors

Durzynska, I.,Uljon, S.,Blacklow, S.C. (deposition date: 2016-08-02, release date: 2017-02-01, Last modification date: 2023-10-04)

Primary citation

Durzynska, I.,Xu, X.,Adelmant, G.,Ficarro, S.B.,Marto, J.A.,Sliz, P.,Uljon, S.,Blacklow, S.C.
STK40 Is a Pseudokinase that Binds the E3 Ubiquitin Ligase COP1.
Structure, 25:287-294, 2017

PubMed Abstract: Serine/threonine kinase 40 (STK40) was originally identified as a distant homolog of Tribbles-family proteins. Despite accumulating data attesting to the importance of STK40 in a variety of different physiologic processes, little is known about its biological activity or mechanism of action. Here, we show that STK40 interacts with Constitutive Photomorphogenic Protein 1 (COP1), relying primarily on a C-terminal sequence analogous to the motif found in Tribbles proteins. In order to further elucidate structure-function relationships in STK40, we determined the crystal structure of the STK40 kinase homology domain at 2.5 Å resolution. The structure, together with ATP-binding assay results, show that STK40 is a pseudokinase, in which substitutions of conserved residues within the kinase domain prevent ATP binding. Although the structure of the kinase homology domain diverges from the analogous region of Trib1, the results reported here suggest functional parallels between STK40 and Tribbles-family proteins as COP1 adaptors.

PubMed: 28089446
DOI: 10.1016/j.str.2016.12.008

Experimental method

X-RAY DIFFRACTION (2.53 Å)