1STC

CAMP-DEPENDENT PROTEIN KINASE, ALPHA-CATALYTIC SUBUNIT IN COMPLEX WITH STAUROSPORINE

Summary for 1STC

• Entry DOI: 10.2210/pdb1stc/pdb
• Descriptor: CAMP-DEPENDENT PROTEIN KINASE, PROTEIN KINASE INHIBITOR, STAUROSPORINE, ... (4 entities in total)
• Functional Keywords: protein kinase, staurosporine, camp, phosphorylation, complex (transferase-inhibitor), serine/threonine-protein kinase, complex (transferase-inhibitor) complex, complex (transferase/inhibitor)
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm: P00517
• Total number of polymer chains: 2
• Total formula weight: 43479.34

Authors

Prade, L.,Engh, R.A.,Girod, A.,Kinzel, V.,Huber, R.,Bossemeyer, D. (deposition date: 1997-10-10, release date: 1998-02-25, Last modification date: 2023-08-09)

Primary citation

Prade, L.,Engh, R.A.,Girod, A.,Kinzel, V.,Huber, R.,Bossemeyer, D.
Staurosporine-induced conformational changes of cAMP-dependent protein kinase catalytic subunit explain inhibitory potential.
Structure, 5:1627-1637, 1997

PubMed Abstract: Staurosporine inhibits most protein kinases at low nanomolar concentrations. As most tyrosine kinases, along with many serine/threonine kinases, are either proto oncoproteins or are involved in oncogenic signaling, the development of protein kinase inhibitors is a primary goal of cancer research. Staurosporine and many of its derivatives have significant biological effects, and are being tested as anticancer drugs. To understand in atomic detail the mode of inhibition and the parameters of high-affinity binding of staurosporine to protein kinases, the molecule was cocrystallized with the catalytic subunit of cAMP-dependent protein kinase.

PubMed: 9438863
DOI: 10.1016/S0969-2126(97)00310-9

Experimental method

X-RAY DIFFRACTION (2.3 Å)