Correlations between secondary structure- and protein–protein interface-mimicry: the interface mimicry hypothesis-Reference-Cited by-同舟云学术

Correlations between secondary structure- and protein–protein interface-mimicry: the interface mimicry hypothesis

Published:2019 Issue:12 Volume:17 Page:3267-3274
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Taechalertpaisarn Jaru¹²³⁴^ORCID,Lyu Rui-Liang¹²³⁴^ORCID,Arancillo Maritess¹²³⁴^ORCID,Lin Chen-Ming¹²³⁴^ORCID,Perez Lisa M.⁵²³⁴,Ioerger Thomas R.⁶²³⁴,Burgess Kevin¹²³⁴^ORCID

Affiliation:

1. Department of Chemistry

2. Texas A & M University

3. College Station

4. USA

5. Laboratory For Molecular Simulation

6. Department of Computer Science

Abstract

Preferred conformations of several peptidomimetics (specifically, minimalist mimics) were elucidated and compared with protein-protein interfaces on a huge scale, leading to a hypothesis regarding how these compounds mimic protein interface segments.

Funder

National Science Foundation

National Institutes of Health

Welch Foundation

U.S. Department of Defense

Cancer Prevention and Research Institute of Texas

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2019/OB/C9OB00204A

Reference34 articles.

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3. Evaluating minimalist mimics by exploring key orientations on secondary structures (EKOS)

4. Terphenyl‐Based Helical Mimetics That Disrupt the p53/HDM2 Interaction

5. Modeling of Arylamide Helix Mimetics in the p53 Peptide Binding Site of hDM2 Suggests Parallel and Anti-Parallel Conformations Are Both Stable

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