Structure and function of the yeast U-box-containing ubiquitin ligase Ufd2p

franklin submitted, created time 1 year 3 months (www.pnas.org)

Proteins conjugated by Lys-48-linked polyubiquitin chains are preferred substrates of the eukaryotic proteasome. Polyubiquitination requires an activating enzyme (E1), a conjugating enzyme (E2), and a ligase (E3).

Submit comment | Blog It | Email It | Keywords: structure function yeast ligase

Solution structure of the A4 domain of factor XI sheds light on the mechanism of zymogen activation

jackson submitted, created time 1 year 3 months (www.pnas.org)

Factor XI (FXI) is a homodimeric blood coagulation protein. Each monomer comprises four tandem apple-domain repeats (A1–A4) and a serine protease domain. We report here the NMR solution structure of the A4 domain (residues 272–361), which mediates formation of the disulfide-linked FXI dimer.

Submit comment | Blog It | Email It | Keywords: factor XI structure A4 domain

Scientists learn structure of enzyme in unusual virus

kitty submitted, created time 1 year 3 months (news.uns.purdue.edu)

Biologists have determined the three-dimensional structure of an unusual viral enzyme that is required in the assembly of new viruses.

3 comments | Blog It | Email It | Keywords: structure virus assembly

Structure and Stability of DNA Watson-Crick Base Pairs and Effects of the Molecular Environment

Researchers use new approach to predict protein function

bianjie submitted, created time 1 year 5 months (www.news.uiuc.edu)

In a paper published online this month in the journal Nature Chemical Biology, researchers report that they have developed a way to determine the function of some of the hundreds of thousands of proteins for which amino acid sequence data are available, but whose structure and function remain unknown.

3 comments | Blog It | Email It | Keywords: protein amino acid sequence structure function

Tumour prevention by a single antibody domain targeting the interaction of signal transduction proteins with RAS

addict submitted, created time 1 year 6 months (www.nature.com)

"We describe a single immunoglobulin variable region domain that specifically binds to activated GTP-bound RAS and prevents RAS-dependent tumorigenesis in a mouse model. The crystal structure of the immunoglobulin–RAS complex shows that the variable region competitively binds to the conformationally variant regions of RAS, where its signalling effector molecules interact. This allows the plasma membrane targeted single domain intrabody to inhibit signalling by mutant RAS

Submit comment | Blog It | Email It | Keywords: human disease intrabody protein–protein interaction RAS structure

COMPUTER-BASED DESIGN OF NOVEL PROTEIN STRUCTURES