How non -imposed protein classes manage biological functions

Researchers have discovered how non -structures of surface protein regularly make the cell biological function. Their study, appeared in Nature communicationsG. Protein, together with the receptors (GPCR), sheds new light on the interaction. It lives in the membranes of almost all the cells in the body. This interaction has an important role in the discovery of drugs.

The joint team is the structural dynamics of the Research Center (CRC) 1423-GPCR activation and signaling with mutual cooperation at the University of Lipzig University and Martin Luther University.

The receptors combined with G protein play a key role in many biological processes and the effects of drugs are very important, for example, those that are used to treat hypertension, pain, allergies or weight loss. Despite deep research, many questions about the work of these important receptors are not answering.

The Y2 receptors testing in the study are activated by peptide hormone neuropathyide Wi (NPY), which affects various processes in the brain.

Researchers of the CRC 1423 investigated the role of the flexible N -terminal segment of the Y2 receptor when the Messenger is connected to the NPY receptor and triggers any reaction in the cell. They found that this cellular partner, especially affects protein arrest 3. It is an important player who determines how the sealed signal responds.

Like many GPCRs, the Y2 receptor has a highly flexible, non -structured N -terminal region whose work is considered poor. “The special thing about this section of the receptor is that it is the same thing that is internally known as the defective region. It is not included in a stable structure, but instead changes its shape permanently.

“You can make it a picture like a cloud that the protein segment moves. It is so fast that it is experimentally difficult to capture individual states and thus they are assigned specific work,” Dr. Anti Kaiser, the University of Lipzig University, and Martin Luther Berg, and Martin Luther Berg, and Luther Berg.

Several research groups joined the forces within the CRC 1423 to investigate these highly complex mechanisms. The use of a technique specially developed for this receptor-connected to the cross-connected cross-attached and a combination of highly sensitive masmicatometry-led Professor Andrea Sins managed to identify the correct locations of the interaction between Y2 receptor and NPY.

It became clear that the receptor’s non -terminal region comes in direct contact with Messenger NPY. This search served as the beginning of a widespread variable studies on receptor to check the work of individual regions.

“We were able to see that a short region of negative charging density is important to ensure stable, lasting hormone binding of peptide hormone. Interestingly, some receptor mediation cellular reactions are fully intact, even with contact with Ann Terminus, however, with contact with the doctrine.

These observations confirmed and further improved professors Jeans Mailor and Peter Holdbrand’s research groups improved with the help of computers using structural modeling and molecular dynamics. “Our understanding of the practical importance of flexible areas in signaling is still in a very early stage,” says Holdbind, a professor at the University of Lipzig University.

Working groups have been conducting joint research in this sector for four years, and these new results have been widely operated. This combined publication makes it more valuable.

“Although there are still no approved medicines that work especially through Y2 receptors, these results provide more construction blocks to get even better understanding of practical procedures in the future and identify new drug goals.”