Scientists have analyzed the crystal structure of MFN1 fragment

It is reported that Professor Gao Song research group from the Zhongshan University Cancer Center center analyzed the crystal structure of MFN1 fragment in different triphosphate guanosine (GTP) hydrolysis condition and clarified the mechanism of MFN1 hydrolysis GTP and proposed MFN1 mitochondrial outer membrane embolization mediated model. Recently, the relevant research has been published online in the journal Nature, which also publishes other studies on recombinant human proteins.

The body consists of tens to hundreds of trillion cells, of which the vast majority of cells contain an important "organ" called "mitochondria" (organelle), which is the "energy plant" of cells. Mitochondrial fusion relies on a protein "machine" implementation called mitofusin. This machine is anchored on the surface of the mitochondria to achieve docking and fusion of different mitochondria by using a small molecule compound "fuel" called GTP. Mitofusin machines sometimes suffer from a "part" failure due to genetic mutations, leading to mitochondrial fusion disorders and the associated human disease.

Researchers use "X-ray crystal diffraction" and other technologies to make mitofusin form as sugar and salt-like crystals (volume only one thousandth of a million) for diffraction experiments. They finally observed microstructure of mitofusin machine and found it can adjust their own structure through the consumption of GTP fuel and can adsorb each other.

The study reveals an important process of basic life activities that has important guiding roles for people to explore the causes of related diseases and to develop appropriate clinical approaches. By the way, Flarebio offers good-quality recombinant proteins like recombinant App at good prices.