Supramolecular protection from the enzymatic tyrosine phosphorylation in a polypeptide-Reference-Cited by-同舟云学术

Supramolecular protection from the enzymatic tyrosine phosphorylation in a polypeptide

Published:2016 Issue:52 Volume:52 Page:8142-8145
ISSN:1359-7345
Container-title:Chemical Communications
language:en
Short-container-title:Chem. Commun.

Author:

Faggi Enrico¹²³⁴,Pérez Yolanda⁵²³⁴,Luis Santiago V.⁶⁷⁸⁴,Alfonso Ignacio¹²³⁴

Affiliation:

1. Department of Biological Chemistry and Molecular Modelling

2. IQAC-CSIC

3. Barcelona

4. Spain

5. NMR Facility

6. Department of Inorganic and Organic Chemistry

7. ESTCE Universitat Jaume I

8. Castellón

Abstract

Two pseudopeptidic cages bind the EYE peptide motif of poly(EY) in buffered water, as shown by NMR and fluorescence spectroscopy. This supramolecular interaction protects the Tyr residues from the enzymatic phosphorylation by PTK.

Publisher

Royal Society of Chemistry (RSC)

Subject

Materials Chemistry,Metals and Alloys,Surfaces, Coatings and Films,General Chemistry,Ceramics and Composites,Electronic, Optical and Magnetic Materials,Catalysis

Link

http://pubs.rsc.org/en/content/articlepdf/2016/CC/C6CC03875A

Reference45 articles.

1. Discovery of Sequence-Selective Peptide Binding by Synthetic Receptors Using Encoded Combinatorial Libraries

2. Peptide and Protein Recognition by Designed Molecules

3. Sequence-Selective Recognition of Peptides within the Single Binding Pocket of a Self-Assembled Coordination Cage

4. Sequence-Selective Peptide Recognition with Designed Modules

5. Molecular Recognition of Lys and Arg Methylation

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