13 Works

Open conformation SHP2

The tyrosine phosphatase SHP2 interconverts between open, active, and closed, inactive, structures to regulate crucial cell signaling pathways. Oncogenic mutations such as E76K shifts the equilibrium towards the open state making SHP2 200 fold more active than WT. In contrast to the closed state of SHP2 that has been well described mainly by crystal structures, the open structure is unknown and possibly adopts a ensemble of states in solution that hampers crystallization. Using homology modeling...

Homology model of Arabidopsis thaliana nitrile-specifier protein 3 (AtNSP3)

Daniela Eisenschmidt-Bönn
Glucosinolates, a group of sulfur-rich thioglucosides found in plants of the order Brassicales, have attracted a lot of interest as chemical defenses of plants and health promoting substances in human diet. They are accumulated separately from their hydrolyzing enzymes, myrosinases, within the intact plant, but undergo myrosinase-catalyzed hydrolysis upon tissue disruption. This results in various biologically active products, e.g. isothiocyanates, simple nitriles, epithionitriles, and organic thiocyanates. While formation of isothiocyanates proceeds by a spontaneous rearrangement...

Allosteres to Regulate Neurotransmitter Sulfonation

Catecholamine neurotransmitter levels in the synapses of the brain shape human disposition — cognitive flexibility, aggression, depression, reward seeking… — and manipulating these levels is a major objective of the pharmaceutical industry. Certain transmitters are extensively sulfonated — an inactivating modification catalyzed by human sulfotransferase 1A3 (SULT1A3). To our knowledge, sulfonation as therapeutic means of regulating transmitter activity has not been explored. Here we describe the discovery of a SULT1A3 allosteric site that can be...

Bacterial condensin O-shape

Dana Krepel Zussman
The structure of the whole bacterial condensin complex, composed of 2924 amino acid at atomic resolution. The structure was obtained from integrative modeling and co-evolutionary information. The complex is composed of 2 identical SMC monomers, a single ScpA protein, and two ScpB subunits. The sequence of SMC correspond to that of Thermotoga maritima while ScpA and B are from Streptococcus pneumoniae.

Bacterial condensin I-shape

Dana Krepel Zussman
The structure of the whole bacterial condensin complex, composed of 2924 amino acid at atomic resolution. The structure was obtained from integrative modeling and co-evolutionary information. The complex is composed of 2 identical SMC monomers, a single ScpA protein, and two ScpB subunits. The sequence of SMC correspond to that of Thermotoga maritima while ScpA and B are from Streptococcus pneumoniae.

Registration Year

  • 2018
    13

Resource Types

  • Model
    13