1SVX

Crystal structure of a designed selected Ankyrin Repeat protein in complex with the Maltose Binding Protein

Summary for 1SVX

• Entry DOI: 10.2210/pdb1svx/pdb
• Related: 1MJ0
• Descriptor: Ankyrin Repeat Protein off7, Maltose-binding periplasmic protein (3 entities in total)
• Functional Keywords: ankyrin repeat protein, selected binder, protein design, artificial complex, de novo protein-sugar binding protein complex, de novo protein/sugar binding protein
• Cellular location: Periplasm: P02928
• Total number of polymer chains: 2
• Total formula weight: 61496.18

Authors

Binz, H.K.,Amstutz, P.,Kohl, A.,Stumpp, M.T.,Briand, C.,Forrer, P.,Gruetter, M.G.,Plueckthun, A. (deposition date: 2004-03-30, release date: 2004-05-25, Last modification date: 2024-02-14)

Primary citation

Binz, H.K.,Amstutz, P.,Kohl, A.,Stumpp, M.T.,Briand, C.,Forrer, P.,Gruetter, M.G.,Plueckthun, A.
High-affinity binders selected from designed ankyrin repeat protein libraries
NAT.BIOTECHNOL., 22:575-582, 2004

PubMed Abstract: We report here the evolution of ankyrin repeat (AR) proteins in vitro for specific, high-affinity target binding. Using a consensus design strategy, we generated combinatorial libraries of AR proteins of varying repeat numbers with diversified binding surfaces. Libraries of two and three repeats, flanked by 'capping repeats,' were used in ribosome-display selections against maltose binding protein (MBP) and two eukaryotic kinases. We rapidly enriched target-specific binders with affinities in the low nanomolar range and determined the crystal structure of one of the selected AR proteins in complex with MBP at 2.3 A resolution. The interaction relies on the randomized positions of the designed AR protein and is comparable to natural, heterodimeric protein-protein interactions. Thus, our AR protein libraries are valuable sources for binding molecules and, because of the very favorable biophysical properties of the designed AR proteins, an attractive alternative to antibody libraries.

PubMed: 15097997
DOI: 10.1038/nbt962

Experimental method

X-RAY DIFFRACTION (2.24 Å)