In silico analysis of interaction pattern switching in ligand⋯receptor binding in Golgi α-mannosidase II induced by the protonated states of inhibitors-Reference-Cited by-同舟云学术

In silico analysis of interaction pattern switching in ligand⋯receptor binding in Golgi α-mannosidase II induced by the protonated states of inhibitors

Published:2017 Issue:19 Volume:19 Page:12527-12537
ISSN:1463-9076
Container-title:Physical Chemistry Chemical Physics
language:en
Short-container-title:Phys. Chem. Chem. Phys.

Author:

Sladek V.¹²³⁴⁵^ORCID,Kóňa J.¹²³⁴,Tokiwa H.⁵⁶⁷⁸

Affiliation:

1. Institute of Chemistry – Centre for Glycomics

2. Slovak Academy of Sciences

3. 845 38 Bratislava

4. Slovakia

5. Dept. of Chemistry

6. Rikkyo University

7. Toshima

8. Japan

Abstract

Different binding modes for charge-neutral and protonated inhibitor forms in Golgi α-mannosidase II active sites may influence their biological activities.

Funder

Ministry of Education, Culture, Sports, Science and Technology

Rikkyo University

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry,General Physics and Astronomy

Link

http://pubs.rsc.org/en/content/articlepdf/2017/CP/C7CP01200D

Reference95 articles.

1. α-Mannosidase as a Zinc-dependent Enzyme

2. Novel mannosidase inhibitor blocking conversion of high mannose to complex oligosaccharides