<HashMap><database>biostudies-literature</database><scores/><additional><omics_type>Unknown</omics_type><volume>96(16)</volume><submitter>Botuyan MV</submitter><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</pubmed_abstract><journal>Proceedings of the National Academy of Sciences of the United States of America</journal><pagination>9033-8</pagination><full_dataset_link>https://www.ebi.ac.uk/biostudies/studies/S-EPMC17727</full_dataset_link><repository>biostudies-literature</repository><pubmed_title>Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C.</pubmed_title><pmcid>PMC17727</pmcid><pubmed_authors>Conaway RC</pubmed_authors><pubmed_authors>Botuyan MV</pubmed_authors><pubmed_authors>Chakrabartty A</pubmed_authors><pubmed_authors>Arrowsmith CH</pubmed_authors><pubmed_authors>Edwards AM</pubmed_authors><pubmed_authors>Chazin WJ</pubmed_authors><pubmed_authors>Conaway JW</pubmed_authors><pubmed_authors>Koth CM</pubmed_authors><pubmed_authors>Mer G</pubmed_authors></additional><is_claimable>false</is_claimable><name>Binding of elongin A or a von Hippel-Lindau peptide stabilizes the structure of yeast elongin C.</name><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</description><dates><release>1999-01-01T00:00:00Z</release><publication>1999 Aug</publication><modification>2025-04-04T10:42:03.759Z</modification><creation>2019-03-26T22:27:57Z</creation></dates><accession>S-EPMC17727</accession><cross_references><pubmed>10430890</pubmed><doi>10.1073/pnas.96.16.9033</doi></cross_references></HashMap>