Literature summary for 1.2.1.104 extracted from

Hezaveh, S.; Zeng, A.P.; Jandt, U.
Investigation of core structure and stability of human pyruvate dehydrogenase complex a coarse-grained approach (2017), ACS Omega, 2, 1134-1145 .

Search for more literature for 1.2.1.104

Crystallization (Commentary)

Crystallization (Comment)	Organism
coarse-grained models of E2/E3BP, the two subunits of the massive pyruvate dehydrogenase complex core. Both subunit models show very good structural stability and consistency with those from the atomistic level. The homotrimers and heterotrimers were modeled, and the full WT 60-meric core of the pyruvate dehydrogenase complex is built up. Exploration of the stability of two substitutional models: 40E2+20E3BP and 48E2+12E3BP shows a higher stability and sphericity for the second model. Simulation of C-terminal truncated E2/E3BP cores of different lengths shows the instability of the core assembly and symmetry due to subunit separations	Homo sapiens

Crystallization (Comment)

Organism

coarse-grained models of E2/E3BP, the two subunits of the massive pyruvate dehydrogenase complex core. Both subunit models show very good structural stability and consistency with those from the atomistic level. The homotrimers and heterotrimers were modeled, and the full WT 60-meric core of the pyruvate dehydrogenase complex is built up. Exploration of the stability of two substitutional models: 40E2+20E3BP and 48E2+12E3BP shows a higher stability and sphericity for the second model. Simulation of C-terminal truncated E2/E3BP cores of different lengths shows the instability of the core assembly and symmetry due to subunit separations

Homo sapiens

Organism

Organism	UniProt	Comment	Textmining
Homo sapiens	-	-	-

Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.

Release 2023.1 (January 2023)