{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["96(16)"],"submitter":["Botuyan MV"],"pubmed_abstract":["Elongin is a heterotrimeric transcription elongation factor composed of subunits A, B, and C in mammals. Elongin A and C are F-box-containing and SKP1 homologue proteins, respectively, and are therefore of interest for their potential roles in cell cycle-dependent proteolysis. Mammalian elongin C interacts with both elongin A and elongin B, as well as with the von Hippel-Lindau tumor suppressor protein VHL. To investigate the corresponding interactions in yeast, we have utilized NMR spectroscopy combined with ultracentrifugal sedimentation experiments to examine complexes of yeast elongin C (Elc1) with yeast elongin A (Ela1) and two peptides from homologous regions of Ela1 and human VHL. Elc1 alone is a homotetramer composed of subunits with a structured N-terminal region and a dynamically"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["9033-8"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC17727"],"repository":["biostudies-literature"],"pubmed_title":["Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C."],"pmcid":["PMC17727"],"pubmed_authors":["Conaway RC","Botuyan MV","Chakrabartty A","Arrowsmith CH","Edwards AM","Chazin WJ","Conaway JW","Koth CM","Mer G"],"additional_accession":[]},"is_claimable":false,"name":"Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C.","description":"Elongin is a heterotrimeric transcription elongation factor composed of subunits A, B, and C in mammals. Elongin A and C are F-box-containing and SKP1 homologue proteins, respectively, and are therefore of interest for their potential roles in cell cycle-dependent proteolysis. Mammalian elongin C interacts with both elongin A and elongin B, as well as with the von Hippel-Lindau tumor suppressor protein VHL. To investigate the corresponding interactions in yeast, we have utilized NMR spectroscopy combined with ultracentrifugal sedimentation experiments to examine complexes of yeast elongin C (Elc1) with yeast elongin A (Ela1) and two peptides from homologous regions of Ela1 and human VHL. Elc1 alone is a homotetramer composed of subunits with a structured N-terminal region and a dynamically","dates":{"release":"1999-01-01T00:00:00Z","publication":"1999 Aug","modification":"2025-04-04T10:42:03.759Z","creation":"2019-03-26T22:27:57Z"},"accession":"S-EPMC17727","cross_references":{"pubmed":["10430890"],"doi":["10.1073/pnas.96.16.9033"]}}