News

NIGMS-funded biologists have solved the structure of an adenosine receptor that could lead to drugs for neurological disorders.

A new window onto the world of protein structure has been opened with the launch of the NIGMS-funded PSI-Nature Structural Genomics Knowledgebase.

An NIGMS-funded collaboration has revealed a key binding pocket for flu infection. Disrupting the interaction could treat flu.

The Protein Structure Initiative has launched an online resource that will enable scientists from across biomedical disciplines to easily access a wealth of information about proteins.

Scientists supported by two major NIH initiatives have captured the first structure of a human G protein-coupled receptor, one of a family of membrane proteins targeted by about half of today's pharmaceuticals.

Now that the Protein Structure Initiative (PSI) has established efficient pipelines for determining the three-dimensional shapes of proteins, it is creating new mechanisms for sharing the resources it has developed with the scientific community.

Two newly funded molecular modeling centers will develop computational methods for reliably predicting protein structures.

A new NIGMS-funded center will improve predictions of three-dimensional protein structures from raw genetic sequence. The center will unite scientists from the Burnham Institute in La Jolla and the University of California, San Diego. 

NIGMS-funded researchers have learned the structure and mechanism of an enzyme that eliminates drugs and toxic compounds from the body. Understanding these details could help reveal why such compounds are not always properly eliminated.

NIGMS-supported scientists have solved the structure of a key protein involved in the infections that strike people with cystic fibrosis. The finding provides a possible drug target for fighting these infections.

Scientists based in Palo Alto, California, have produced brilliant X-ray light from a device just a fraction of the standard size. The advance could transform numerous fields of biomedical research by vastly improving access to a key resource for studying the properties of molecules.

Biochemists have uncovered a new type of protein movement and dubbed it the 'backrub' motion. The team believes the subtle gyration influences proteins' activities in the cell.

Researchers led by Nobel Prize winner Roderick MacKinnon, M.D., of Rockefeller University have used yeast to express and obtain the structure of a mammalian voltage-dependent potassium ion channel—a type of membrane protein that helps transmit electrical signals into and out of heart and nerve cells.

The Protein Structure Initiative, an NIGMS program aimed at determining the three-dimensional shapes of a wide range of proteins, has now determined more than 1,000 different structures.  These structures will shed light on how proteins function in many life processes and could lead to targets for the development of new medicines.