Open AccessStructure of a cyclin‐dependent kinase from Giardia lamblia
Author(s) -
Leibly David J.,
Newling Paul A.,
Abendroth Jan,
Guo Wenjin,
Kelley Angela,
Stewart Lance J.,
Van Voorhis Wesley
Publication year - 2011
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111018070
Subject(s) - cyclin dependent kinase , kinase , biology , giardia lamblia , cyclin dependent kinase 2 , cyclin dependent kinase complex , microbiology and biotechnology , cyclin , protein kinase a , biochemistry , cell cycle , cell
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 ( Gl CDK; 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 Gl CDK with its associated cyclin was not solved, the 1.85 Å resolution structure of apo Gl CDK and a 2.0 Å resolution structure of Gl CDK in complex with adenosine monophosphate are presented and the structural differences from the orthologous human CDK2 and CDK3 are discussed.