[NMR paper] A combination of solid-state NMR and MD simulations reveals the binding mode of a rhomboid protease inhibitor
A combination of solid-state NMR and MD simulations reveals the binding mode of a rhomboid protease inhibitor
Intramembrane proteolysis plays a fundamental role in many biological and pathological processes. Intramembrane proteases thus represent promising pharmacological targets, but few selective inhibitors have been identified. This is in contrast to their soluble counterparts, which are inhibited by many common drugs, and is in part explained by the inherent difficulty to characterize the binding of drug-like molecules to membrane proteins at atomic resolution. Here, we investigated...
nmrlearner
Journal club
0
10-27-2021 10:50 PM
[NMR paper] Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR.
Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles Structure and Dynamics of the Rhomboid Protease GlpG in Liposomes Studied by Solid-State NMR.
J Am Chem Soc. 2019 10 30;141(43):17314-17321
Authors: Shi C, Öster C, Bohg C, Li L, Lange S, Chevelkov V, Lange A
Abstract
Rhomboid proteases are intramembrane proteases that hydrolyze substrate peptide bonds within...
nmrlearner
Journal club
0
11-07-2020 03:20 PM
[ASAP] High-Affinity Binding of LDL Receptor-Related Protein 1 to Matrix Metalloprotease 1 Requires Protease:Inhibitor Complex Formation
High-Affinity Binding of LDL Receptor-Related Protein 1 to Matrix Metalloprotease 1 Requires Protease:Inhibitor Complex Formation
https://pubs.acs.org/na101/home/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.0c00442/20200806/images/medium/bi0c00442_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.0c00442
http://feeds.feedburner.com/~r/acs/bichaw/~4/nOWuoxRNqx8
More...
nmrlearner
Journal club
0
08-07-2020 02:42 AM
Solution NMR Structure and Backbone Dynamics of PartiallyDisordered Arabidopsis thaliana Phloem Protein 16-1,a Putative mRNA Transporter
Solution NMR Structure and Backbone Dynamics of PartiallyDisordered Arabidopsis thaliana Phloem Protein 16-1,a Putative mRNA Transporter
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b01071/20180125/images/medium/bi-2017-01071p_0010.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b01071
http://feeds.feedburner.com/~ff/acs/bichaw?d=yIl2AUoC8zA
http://feeds.feedburner.com/~r/acs/bichaw/~4/8sgEPJHqfXA
More...
nmrlearner
Journal club
0
01-27-2018 12:19 AM
[NMR paper] Solution NMR Structure and Backbone Dynamics of the Partially Disordered Arabidopsis thaliana Phloem Protein 16-1, A Putative mRNA Transporter.
Solution NMR Structure and Backbone Dynamics of the Partially Disordered Arabidopsis thaliana Phloem Protein 16-1, A Putative mRNA Transporter.
Solution NMR Structure and Backbone Dynamics of the Partially Disordered Arabidopsis thaliana Phloem Protein 16-1, A Putative mRNA Transporter.
Biochemistry. 2018 Jan 10;:
Authors: Sashi P, Singarapu KK, Bhuyan AK
Abstract
Although RNA-binding proteins in plant phloem are believed to carry out long-distance systemic transport of RNA in the phloem conduit, the structure of none of them is...
[NMR paper] Solution-state NMR structure of the putative morphogene protein BolA (PFE0790c) from Plasmodium falciparum.
Solution-state NMR structure of the putative morphogene protein BolA (PFE0790c) from Plasmodium falciparum.
Related Articles Solution-state NMR structure of the putative morphogene protein BolA (PFE0790c) from Plasmodium falciparum.
Acta Crystallogr F Struct Biol Commun. 2015 May 1;71(Pt 5):514-521
Authors: Buchko GW, Yee A, Semesi A, Myler PJ, Arrowsmith CH, Hui R
Abstract
Protozoa of the genus Plasmodium are responsible for malaria, which is perhaps the most important parasitic disease to infect mankind. The emergence of...
nmrlearner
Journal club
0
05-07-2015 03:04 PM
NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermo
NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
Related Articles NMR and X-ray structures of the putative sterol carrier protein 2 from Thermus thermophilus HB8 show conformational changes.
J Struct Funct Genomics. 2010 Oct 5;
Authors: Goroncy AK, Murayama K, Shirouzu M, Kuramitsu S, Kigawa T, Yokoyama S
Sterol carrier protein 2 (SCP-2), also known as nonspecific lipid transfer protein, is a ubiquitous intracellular ~13*kDa protein found in mammals, insects, plants,...
![[ASAP] Putative Protein Interactome of the Rhomboid Protease RHBDL4](http://www.bionmr.com/forum/iconimages/journal-club-9/%5Basap%5D-putative-protein-interactome-rhomboid-protease-rhbdl4_ltr.gif)
[ASAP] Putative Protein Interactome of the Rhomboid Protease RHBDL4
Linear Mode
