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Docking and molecular dynamics simulations of the Fyn-SH3 domain with free and phospholipid bilayer-associated 18.5-kDa myelin basic protein (MBP) – Insights into a non-canonical and fuzzy interaction

Title: Docking and molecular dynamics simulations of the Fyn-SH3 domain with free and phospholipid bilayer-associated 18.5-kDa myelin basic protein (MBP) – Insights into a non-canonical and fuzzy interaction
Authors: Bessonov, Kyrylo; Harauz, George; Vassall, Kenrick
Source: Proteins (2017-04-12)
Publisher Information: Wiley Liss, Inc.
Publication Year: 2017
Collection: University of Liège: ORBi (Open Repository and Bibliography)
Subject Terms: molecular dynamics; MBP; docking; Life sciences; Biochemistry; biophysics & molecular biology; Sciences du vivant; Biochimie; biophysique & biologie moléculaire
Description: peer reviewed ; The molecular details of the association between the human Fyn-SH3 domain, and the fragment of 18.5-kDa myelin basic protein (MBP) spanning residues S38–S107 (denoted as xα2-peptide, murine sequence numbering), were studied in silico via docking and molecular dynamics over 50-ns trajectories. The results show that interaction between the two proteins is energetically favorable and heavily-dependent on the MBP proline-rich region (P93-P98) in both aqueous and membrane environments. In aqueous conditions, the xα2-peptide/Fyn-SH3 complex adopts a “sandwich”-like structure. In the membrane context, the xα2-peptide interacts with the Fyn-SH3 domain via the proline-rich region and the β-sheets of Fyn-SH3, with the latter wrapping around the proline-rich region in a form of a clip. Moreover, the simulations corroborate prior experimental evidence of the importance of upstream segments beyond the canonical SH3-ligand. This study thus provides a more-detailed glimpse into the context-dependent interaction dynamics and importance of the β-sheets in Fyn-SH3 and proline-rich region of MBP.
Document Type: article in journal/newspaper
Language: English
ISSN: 0887-3585; 1097-0134
Relation: https://www.synapse.org/#!Synapse:syn5303692/files/; urn:issn:0887-3585; urn:issn:1097-0134; https://orbi.uliege.be/handle/2268/209450; info:hdl:2268/209450; https://orbi.uliege.be/bitstream/2268/209450/1/Fyn_MBP_R1_2017_02_27.pdf; info:pmid:28380689
DOI: 10.1002/prot.25295
Availability: https://orbi.uliege.be/handle/2268/209450; https://orbi.uliege.be/bitstream/2268/209450/1/Fyn_MBP_R1_2017_02_27.pdf; https://doi.org/10.1002/prot.25295
Rights: open access ; http://purl.org/coar/access_right/c_abf2 ; info:eu-repo/semantics/openAccess
Accession Number: edsbas.EA33649F
Database: BASE