期刊
BIOPHYSICAL JOURNAL
卷 100, 期 9, 页码 L50-L52出版社
CELL PRESS
DOI: 10.1016/j.bpj.2011.03.035
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类别
资金
- National Science Foundation [MCB-0845216, TG-MCB070090]
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0845216] Funding Source: National Science Foundation
Using explicit solvent molecular dynamics simulations, we were able to obtain direct observations of shifts in the hydrogen-bonding register of an intermolecular beta-sheet protein-peptide complex. The beta-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 beta-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 beta-sheets.
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