Next Article in Journal
One-Pot Chemoenzymatic Multicomponent Synthesis of Thiazole Derivatives
Next Article in Special Issue
Solution Structure of the Circular γ-Domain Analog from the Wheat Metallothionein Ec-1
Previous Article in Journal
A Piston-Rotaxane with Two Potential Stripes: Force Transitions and Yield Stresses
Previous Article in Special Issue
The Involvement of Amino Acid Side Chains in Shielding the Nickel Coordination Site: An NMR Study
Article Menu

Export Article

Open AccessReview
Molecules 2013, 18(11), 13410-13424; doi:10.3390/molecules181113410

NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review

Research Institute of Pharmaceutical Sciences, College of Pharmacy, Seoul National University, Seoul 151-742, Korea
*
Author to whom correspondence should be addressed.
Received: 21 June 2013 / Revised: 24 October 2013 / Accepted: 27 October 2013 / Published: 30 October 2013
(This article belongs to the Special Issue NMR of Proteins and Small Biomolecules)
View Full-Text   |   Download PDF [588 KB, uploaded 18 June 2014]   |  

Abstract

Due to the widespread and increasing appearance of antibiotic resistance, a new strategy is needed for developing novel antibiotics. Especially, there are no specific antibiotics for Helicobacter pylori (H. pylori). H. pylori are bacteria that live in the stomach and are related to many serious gastric problems such as peptic ulcers, chronic gastritis, mucosa-associated lymphoid tissue lymphoma, and gastric cancer. Because of its importance as a human pathogen, it’s worth studying the structure and function of the proteins from H. pylori. After the sequencing of the H. pylori strain 26695 in 1997, more than 1,600 genes were identified from H. pylori. Until now, the structures of 334 proteins from H. pylori have been determined. Among them, 309 structures were determined by X-ray crystallography and 25 structures by Nuclear Magnetic Resonance (NMR), respectively. Overall, the structures of large proteins were determined by X-ray crystallography and those of small proteins by NMR. In our lab, we have studied the structural and functional characteristics of small proteins from H. pylori. In this review, 25 NMR structures of H. pylori proteins will be introduced and their structure-function relationships will be discussed.
Keywords: Helicobacter pylori; antimicrobial peptides (AMPs); antibiotics; nuclear magnetic resonance (NMR); structure-activity relationship (SAR) Helicobacter pylori; antimicrobial peptides (AMPs); antibiotics; nuclear magnetic resonance (NMR); structure-activity relationship (SAR)
This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Kang, S.-J.; Kim, D.-H.; Lee, B.-J. NMR Study on Small Proteins from Helicobacter pylori for Antibiotic Target Discovery: A Review. Molecules 2013, 18, 13410-13424.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Molecules EISSN 1420-3049 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top