English
 
Help Privacy Policy Disclaimer
  Advanced SearchBrowse

Item

ITEM ACTIONSEXPORT
  Interaction of Cu(i) with the Met-X3-Met motif of alpha-synuclein: Binding ligands, affinity and structural features.

Gentile, I., Garro, H. A., Delgado Ocaña, S., Gonzalez, N., Strohäker, T., Schibich, D., et al. (2018). Interaction of Cu(i) with the Met-X3-Met motif of alpha-synuclein: Binding ligands, affinity and structural features. Metallomics, 10(10), 1383-1389. doi:10.1039/c8mt00232k.

Item is

Files

show Files
hide Files
:
3001166.pdf (Publisher version), 3MB
Name:
3001166.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
:
3001166_Suppl.pdf (Supplementary material), 258KB
Name:
3001166_Suppl.pdf
Description:
-
OA-Status:
Visibility:
Public
MIME-Type / Checksum:
application/pdf / [MD5]
Technical Metadata:
Copyright Date:
-
Copyright Info:
-
License:
-

Locators

show

Creators

show
hide
 Creators:
Gentile, I., Author
Garro, H. A., Author
Delgado Ocaña, S., Author
Gonzalez, N., Author
Strohäker, T.1, Author           
Schibich, D., Author
Quintanar, L., Author
Sambrotta, L., Author
Zweckstetter, M.1, Author           
Griesinger, C.2, Author                 
Menacho Márqueza, M., Author
Fernandez, C. O.2, Author           
Affiliations:
1Research Group of Protein Structure Determination using NMR, MPI for biophysical chemistry, Max Planck Society, ou_578571              
2Department of NMR Based Structural Biology, MPI for biophysical chemistry, Max Planck Society, ou_578567              

Content

show
hide
Free keywords: -
 Abstract: The identity of the Cu(i) binding ligands at Met-X3-Met site of AcαS and its role into the affinity and structural properties of the interaction were elucidated by NMR spectroscopy. We provide evidence that the source of ligands for Cu(i) binding to the Met-X3-Met site comes from the N-terminal acetyl group and the Met-1, Asp-2 and Met-5 residues. From the study of site-directed mutants and synthetic peptide models of αS we demonstrated the critical role played by Met-1 and Met-5 residues on the binding affinity of the Cu(i) complex, acting as the main metal anchoring residues. While having a more modest impact in the affinity features of Cu(i) binding, as compared to the Met residues, the N-terminal acetyl group and Asp-2 are important in promoting local helical conformations, contributing to the stabilization of these structures by favoring Cu(i) binding.

Details

show
hide
Language(s): eng - English
 Dates: 2018-09-242018-10-17
 Publication Status: Issued
 Pages: -
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1039/c8mt00232k
 Degree: -

Event

show

Legal Case

show

Project information

show

Source 1

show
hide
Title: Metallomics
Source Genre: Journal
 Creator(s):
Affiliations:
Publ. Info: -
Pages: - Volume / Issue: 10 (10) Sequence Number: - Start / End Page: 1383 - 1389 Identifier: -