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2KW6

Solution NMR Structure of Cyclin-dependent kinase 2-associated protein 1 (CDK2-associated protein 1; oral cancer suppressor Deleted in oral cancer 1, DOC-1) from H.sapiens, Northeast Structural Genomics Consortium Target Target HR3057H

Summary for 2KW6
Entry DOI10.2210/pdb2kw6/pdb
NMR InformationBMRB: 16808
DescriptorCyclin-dependent kinase 2-associated protein 1 (1 entity in total)
Functional Keywordsstructural genomics, northeast structural genomics consortium (nesg), psi-2, protein structure initiative, cancer suppressor, cell cycle
Biological sourceHomo sapiens (human)
Total number of polymer chains2
Total formula weight14881.08
Authors
Primary citationErtekin, A.,Aramini, J.M.,Rossi, P.,Leonard, P.G.,Janjua, H.,Xiao, R.,Maglaqui, M.,Lee, H.W.,Prestegard, J.H.,Montelione, G.T.
Human cyclin-dependent kinase 2-associated protein 1 (CDK2AP1) is dimeric in its disulfide-reduced state, with natively disordered N-terminal region.
J.Biol.Chem., 287:16541-16549, 2012
Cited by
PubMed Abstract: CDK2AP1 (cyclin-dependent kinase 2-associated protein 1), corresponding to the gene doc-1 (deleted in oral cancer 1), is a tumor suppressor protein. The doc-1 gene is absent or down-regulated in hamster oral cancer cells and in many other cancer cell types. The ubiquitously expressed CDK2AP1 protein is the only known specific inhibitor of CDK2, making it an important component of cell cycle regulation during G(1)-to-S phase transition. Here, we report the solution structure of CDK2AP1 by combined methods of solution state NMR and amide hydrogen/deuterium exchange measurements with mass spectrometry. The homodimeric structure of CDK2AP1 includes an intrinsically disordered 60-residue N-terminal region and a four-helix bundle dimeric structure with reduced Cys-105 in the C-terminal region. The Cys-105 residues are, however, poised for disulfide bond formation. CDK2AP1 is phosphorylated at a conserved Ser-46 site in the N-terminal "intrinsically disordered" region by IκB kinase ε.
PubMed: 22427660
DOI: 10.1074/jbc.M112.343863
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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