ArticleProceedings of the National Academy of Sciences of the United States of America1995
Crystal structure of the cell cycle-regulatory protein suc1 reveals a beta-hinge conformational switch.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 64 citations in OpenAlex.
- Efficacy and safety comparison between R-CHOP and modified NHL-BFM-90 regimens in children and adolescents with diffuse large B-cell lymphoma.Annals of hematology · 2022Article
- Passenger sequences can promote interlaced dimers in a common variant of the maltose-binding protein.Scientific reports · 2019Article
- Exploring the Roles of Proline in Three-Dimensional Domain Swapping from Structure Analysis and Molecular Dynamics Simulations.The protein journal · 2018Article
- Article
- The Prozone Effect Accounts for the Paradoxical Function of the Cdk-Binding Protein Suc1/Cks.Cell reports · 2016Article
- The biochemistry of mitosis.Cold Spring Harbor perspectives in biology · 2015Review
- Conformational dynamics of the focal adhesion targeting domain control specific functions of focal adhesion kinase in cells.The Journal of biological chemistry · 2015Article
- The quaternary structure of the recombinant bovine odorant-binding protein is modulated by chemical denaturants.PloS one · 2014Article
- Cks confers specificity to phosphorylation-dependent CDK signaling pathways.Nature structural & molecular biology · 2013Article
- Domain swapping and amyloid fibril conformation.Prion · 2012Article
- How focal adhesion kinase achieves regulation by linking ligand binding, localization and action.Current opinion in structural biology · 2011Review
- Preliminary crystallographic analysis of the Cks protein p13(suc1P90AP92A) from Schizosacharromyces pombe.European biophysics journal : EBJ · 2005Article
- Control of domain swapping in bovine odorant-binding protein.The Biochemical journal · 2002Article
- Assignment of the 1H, 13C and 15N resonances and secondary structure of the monomeric p13suc1 protein of Saccharomyces pombe.Journal of biomolecular NMR · 2002Article
- Three-dimensional domain swapping in p13suc1 occurs in the unfolded state and is controlled by conserved proline residues.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 1998Review
- Cyclin-stimulated binding of Cks proteins to cyclin-dependent kinases.Molecular and cellular biology · 1998Article
- Mechanism and evolution of protein dimerization.Protein science : a publication of the Protein Society · 1998Article
- Inhibition of parvovirus minute virus of mice replication by a peptide involved in the oligomerization of nonstructural protein NS1.Journal of virology · 1997Article
- Leishmania mexicana p12cks1, a homologue of fission yeast p13suc1, associates with a stage-regulated histone H1 kinase.The Biochemical journal · 1996Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Schizosaccharomyces pombe cell cycle-regulatory protein suc1, named as the suppressor of cdc2 temperature-sensitive mutations, is essential for cell cycle progression. To understand suc1 structure-function relationships and to help resolve conflicting interpretations of suc1 function based on genetic studies of suc1 and its functional homologs in both lower and higher eukaryotes, we have determined the crystal structure of the beta-interchanged suc1 dimer. Each domain consists of three alpha-helices and a four-stranded beta-sheet, completed by the interchange of terminal beta-strands between the two subunits. This beta-interchanged suc1 dimer, when compared with the beta-hairpin single-domain folds of suc1, reveals a beta-hinge motif formed by the conserved amino acid sequence HVPEPH. This beta-hinge mediates the subunit conformation and assembly of suc1: closing produces the intrasubunit beta-hairpin and single-domain fold, whereas opening leads to the intersubunit beta-strand interchange and interlocked dimer assembly reported here. This conformational switch markedly changes the surface accessibility of sequence-conserved residues available for recognition of cyclin-dependent kinase, suggesting a structural mechanism for beta-hinge-mediated regulation of suc1 biological function. Thus, suc1 belongs to the family of domain-swapping proteins, consisting of intertwined and dimeric protein structures in which the dual assembly modes regulate their function.
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