{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Panteva MT"],"funding":["NIGMS NIH HHS"],"pagination":["L50-2"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC3149256"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["100(9)"],"pubmed_abstract":["Using explicit solvent molecular dynamics simulations, we were able to obtain direct observations of shifts in the hydrogen-bonding register of an intermolecular ?-sheet protein-peptide complex. The ?-sheet is formed between the FHA domain of cancer marker protein Ki67 (Ki67FHA) and a peptide fragment of the hNIFK signaling protein. Potential encounter complexes of the Ki67FHA receptor and hNIFK peptide are misregistered states of the ?-sheet. Rearrangements of one of these misregistered states to the native state were captured in three independent simulations. All three rearrangements occurred by a common mechanism: an aromatic residue of the peptide (F263) anchors into a transient hydrophobic pocket of the receptor to facilitate the formation of native hydrogen bonds. To our knowledge, these simulations provide the first atomically detailed visualizations of a mechanism by which nature might correct for errors in the alignment of intermolecular ?-sheets."],"journal":["Biophysical journal"],"pubmed_title":["Direct observations of shifts in the ?-sheet register of a protein-peptide complex using explicit solvent simulations."],"pmcid":["PMC3149256"],"funding_grant_id":["R01 GM062868","R01-GM062868"],"pubmed_authors":["Panteva MT","Bhattacharjee M","Salari R","Chong LT"],"additional_accession":[]},"is_claimable":false,"name":"Direct observations of shifts in the ?-sheet register of a protein-peptide complex using explicit solvent simulations.","description":"Using explicit solvent molecular dynamics simulations, we were able to obtain direct observations of shifts in the hydrogen-bonding register of an intermolecular ?-sheet protein-peptide complex. The ?-sheet is formed between the FHA domain of cancer marker protein Ki67 (Ki67FHA) and a peptide fragment of the hNIFK signaling protein. Potential encounter complexes of the Ki67FHA receptor and hNIFK peptide are misregistered states of the ?-sheet. Rearrangements of one of these misregistered states to the native state were captured in three independent simulations. All three rearrangements occurred by a common mechanism: an aromatic residue of the peptide (F263) anchors into a transient hydrophobic pocket of the receptor to facilitate the formation of native hydrogen bonds. To our knowledge, these simulations provide the first atomically detailed visualizations of a mechanism by which nature might correct for errors in the alignment of intermolecular ?-sheets.","dates":{"release":"2011-01-01T00:00:00Z","publication":"2011 May","modification":"2021-02-20T21:59:28Z","creation":"2019-03-27T03:07:41Z"},"accession":"S-EPMC3149256","cross_references":{"pubmed":["21539773"],"doi":["10.1016/j.bpj.2011.03.035"]}}