3GC0

Structure of the CMGC CDK Kinase from Giardia lamblia in complex with AMP

Summary for 3GC0

• Entry DOI: 10.2210/pdb3gc0/pdb
• Descriptor: Kinase, CMGC CDK, ADENOSINE MONOPHOSPHATE (3 entities in total)
• Functional Keywords: ssgcid, kinase, cmgc cdk, amp, atp-binding, nucleotide-binding, serine/threonine-protein kinase, transferase, structural genomics, seattle structural genomics center for infectious disease
• Biological source: Giardia lamblia
• Total number of polymer chains: 1
• Total formula weight: 37924.34

Authors

Seattle Structural Genomics Center for Infectious Disease (SSGCID) (deposition date: 2009-02-20, release date: 2009-03-24, Last modification date: 2023-09-06)

Primary citation

Leibly, D.J.,Newling, P.A.,Abendroth, J.,Guo, W.,Kelley, A.,Stewart, L.J.,Van Voorhis, W.
Structure of a cyclin-dependent kinase from Giardia lamblia.
Acta Crystallogr.,Sect.F, 67:1084-1089, 2011

PubMed Abstract: Giardia lamblia is the etiologic agent of giardiasis, a water-borne infection that is prevalent throughout the world. The need for new therapeutics for the treatment of giardiasis is of paramount importance. Owing to the ubiquitous nature of kinases and their vital importance in organisms, they are potential drug targets. In this paper, the first structure of a cyclin-dependent kinase (CDK) from G. lamblia (GlCDK; UniProt A8BZ95) is presented. CDKs are cell-cycle-associated kinases that are actively being pursued as targets for anticancer drugs as well as for antiparasitic chemotherapy. Generally, a CDK forms a complex with its associated cyclin. This CDK-cyclin complex is active and acts as a serine/threonine protein kinase. Typically, CDKs are responsible for the transition to the next phase of the cell cycle. Although the structure of GlCDK with its associated cyclin was not solved, the 1.85 Å resolution structure of apo GlCDK and a 2.0 Å resolution structure of GlCDK in complex with adenosine monophosphate are presented and the structural differences from the orthologous human CDK2 and CDK3 are discussed.

PubMed: 21904054
DOI: 10.1107/S1744309111018070

Experimental method

X-RAY DIFFRACTION (2 Å)