Linked Life Data

19320462

Source:http://linkedlifedata.com/resource/pubmed/id/19320462

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
19
pubmed:dateCreated
2009-5-12
pubmed:abstractText
Ankyrin repeat (AR) proteins are one of the most abundant repeat protein classes in nature, and they are involved in numerous physiological processes through mediating protein/protein interactions. The repetitive and modular architecture of these AR proteins may lead to biochemical and biophysical properties distinct from those of globular proteins. It has been demonstrated that like most globular proteins, AR proteins exhibit a two-state, cooperative transition in chemical- and heat-induced unfolding. However, the biophysical characteristics underlying such cooperative unfolding remain to be further investigated. In the present study, we evaluated the conformational stability of a group of cyclin-dependent kinase (CDK) 4-interacting AR proteins, P16, P18, IkappaBalpha, gankyrin, and their truncated mutants under different conditions, including the presence of denaturants, temperature, and pH. Our results showed that the first four N-terminal ARs are required to form a potent and stable CDK4 modulator. Moreover, in spite of their similarities in skeleton structure, CDK4 binding, and cooperative unfolding, P16, P18, IkappaBalpha, and gankyrin exhibited considerably different biophysical properties with regard to the conformational stability, and these differences mainly resulted from the discrepancies in the primary sequence of the relatively conserved AR motifs. Our results also demonstrated that these sequence discrepancies are able to influence the function of AR proteins to a certain extent. Overall, our results provide important insights into understanding the biophysical properties of AR proteins.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
1520-4995
pubmed:author
pubmed:issnType
Electronic
pubmed:day
19
pubmed:volume
48
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
4050-62
pubmed:dateRevised
2010-11-18
pubmed:meshHeading
pubmed-meshheading:19320462-Amino Acid Motifs, pubmed-meshheading:19320462-Amino Acid Sequence, pubmed-meshheading:19320462-Ankyrin Repeat, pubmed-meshheading:19320462-Conserved Sequence, pubmed-meshheading:19320462-Cyclin-Dependent Kinase 2, pubmed-meshheading:19320462-Cyclin-Dependent Kinase 4, pubmed-meshheading:19320462-Gadolinium, pubmed-meshheading:19320462-Glutathione Transferase, pubmed-meshheading:19320462-Histidine, pubmed-meshheading:19320462-Humans, pubmed-meshheading:19320462-Hydrogen-Ion Concentration, pubmed-meshheading:19320462-Hydrophobic and Hydrophilic Interactions, pubmed-meshheading:19320462-Models, Biological, pubmed-meshheading:19320462-Models, Molecular, pubmed-meshheading:19320462-Molecular Sequence Data, pubmed-meshheading:19320462-Protein Conformation, pubmed-meshheading:19320462-Protein Denaturation, pubmed-meshheading:19320462-Protein Structure, Secondary, pubmed-meshheading:19320462-Protein Structure, Tertiary, pubmed-meshheading:19320462-Recombinant Fusion Proteins, pubmed-meshheading:19320462-Temperature
pubmed:year
2009
pubmed:articleTitle
Comparisons of the conformational stability of cyclin-dependent kinase (CDK) 4-interacting ankyrin repeat (AR) proteins.
pubmed:affiliation
Ohio State Biochemistry Program, The Ohio State University, Columbus, Ohio 43210, USA.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, N.I.H., Extramural