Main Page

Huddy, Hsia, Kibler, Xu & 27 others in the Nobel Prize winning group of David Baker have designed standardized protein building blocks that self assemble into a wide range of nanostructures. The building blocks attach to each other at engineered sites and angles, and come in various sizes.

>>> Get a quick overview! >>>

IB Tomasic, MC Metcalf, AI Guce, NE Clark, SC Garman. J. Biol. Chem. 2010 doi: 10.1074/jbc.M110.118588
The human lysosomal enzymes α-galactosidase and α-N-acetylgalactosaminidase share 46% amino acid sequence identity and have similar folds. Using a rational protein engineering approach, we interconverted the enzymatic specificity of α-GAL and α-NAGAL. The engineered α-GAL retains the antigenicity but has acquired the enzymatic specificity of α-NAGAL. Conversely, the engineered α-NAGAL retains the antigenicity but has acquired the enzymatic specificity of the α-GAL enzyme. Comparison of the crystal structures of the designed enzyme to the wild-type enzymes shows that active sites superimpose well, indicating success of the rational design. The designed enzymes might be useful as non-immunogenic alternatives in enzyme replacement therapy for treatment of lysosomal storage disorders such as Fabry disease.

>>> Visit this I3DC complement >>>

Above is an integral membrane protein that takes up, into your intestinal cells, orally consumed peptide nutrients and drugs. Its lumen-face (top) opens and binds peptide or drug (small solid object in the center), then closes, while its cytoplasmic face (bottom) opens to release its cargo into the intestinal cell, which passes it on to the blood circulation.

>>> See more animations and explanation >>>