Matches in UGent Biblio for { <https://biblio.ugent.be/publication/153984#aggregation> ?p ?o. }
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- aggregation classification "A1".
- aggregation creator B55484.
- aggregation creator B55485.
- aggregation creator B55486.
- aggregation creator B55487.
- aggregation creator B55488.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation creator person.
- aggregation date "2002".
- aggregation format "application/pdf".
- aggregation hasFormat 153984.bibtex.
- aggregation hasFormat 153984.csv.
- aggregation hasFormat 153984.dc.
- aggregation hasFormat 153984.didl.
- aggregation hasFormat 153984.doc.
- aggregation hasFormat 153984.json.
- aggregation hasFormat 153984.mets.
- aggregation hasFormat 153984.mods.
- aggregation hasFormat 153984.rdf.
- aggregation hasFormat 153984.ris.
- aggregation hasFormat 153984.txt.
- aggregation hasFormat 153984.xls.
- aggregation hasFormat 153984.yaml.
- aggregation isPartOf urn:issn:0021-9258.
- aggregation language "eng".
- aggregation rights "I have transferred the copyright for this publication to the publisher".
- aggregation subject "Biology and Life Sciences".
- aggregation title "Solution NMR study of the monomeric form of p13suc1 protein sheds light on the hinge region determining the affinity for a phosphorylated substrate".
- aggregation abstract "Cyclin-dependent kinase subunit (CKS) proteins bind to cyclin-dependent kinases and target various proteins to phosphorylation and proteolysis during cell division. Crystal structures showed that CKS can exist both in a closed monomeric conformation when bound to the kinase and in an inactive C-terminal beta-strand-exchanged conformation. With the exception of the hinge loop, however, both crystal structures are identical, and no new protein interface is formed in the dimer. Protein engineering studies have pinpointed the crucial role of the proline 90 residue of the p13(suc1) CKS protein from Schizosaccharomyces pombe in the monomer-dimer equilibrium and have led to the concept of a loaded molecular spring of the beta-hinge motif. Mutation of this hinge proline into an alanine stabilizes the protein and prevents the occurrence of swapping. However, other mutations further away from the hinge as well as ligand binding can equally shift the equilibrium between monomer and dimer. To address the question of differential affinity through relief of the strain, here we compare the ligand binding of the monomeric form of wild-type S. pombe p13(suc1) and its hinge mutant P90A in solution by NMR spectroscopy. We indeed observed a 5-fold difference in affinity with the wild-type protein being the most strongly binding. Our structural study further indicates that both wild-type and the P90A mutant proteins adopt in solution the closed conformation but display different dynamic properties in the C-terminal beta-sheet involved in domain swapping and protein interactions.".
- aggregation authorList BK141062.
- aggregation endPage "12381".
- aggregation issue "14".
- aggregation startPage "12375".
- aggregation volume "277".
- aggregation aggregates 4146480.
- aggregation isDescribedBy 153984.
- aggregation similarTo jbc.M111741200.
- aggregation similarTo LU-153984.