3ZY7

Crystal structure of computationally redesigned gamma-adaptin appendage domain forming a symmetric homodimer

Summary for 3ZY7

• Entry DOI: 10.2210/pdb3zy7/pdb
• Related: 1GYU 1GYV 1GYW 1W63 2A7B
• Descriptor: AP-1 COMPLEX SUBUNIT GAMMA-1, ISOPROPYL ALCOHOL, DI(HYDROXYETHYL)ETHER, ... (4 entities in total)
• Functional Keywords: endocytosis, protein design, computational design
• Biological source: MUS MUSCULUS (HOUSE MOUSE)
• Cellular location: Golgi apparatus: P22892
• Total number of polymer chains: 2
• Total formula weight: 27607.30

Authors

Stranges, P.B.,Machius, M.,Miley, M.J.,Tripathy, A.,Kuhlman, B. (deposition date: 2011-08-17, release date: 2011-12-28, Last modification date: 2023-12-20)

Primary citation

Stranges, P.B.,Machius, M.,Miley, M.J.,Tripathy, A.,Kuhlman, B.
Computational Design of a Symmetric Homodimer Using Beta-Strand Assembly.
Proc.Natl.Acad.Sci.USA, 108:20562-, 2011

PubMed Abstract: Computational design of novel protein-protein interfaces is a test of our understanding of protein interactions and has the potential to allow modification of cellular physiology. Methods for designing high-affinity interactions that adopt a predetermined binding mode have proved elusive, suggesting the need for new strategies that simplify the design process. A solvent-exposed backbone on a β-strand is thought of as "sticky" and β-strand pairing stabilizes many naturally occurring protein complexes. Here, we computationally redesign a monomeric protein to form a symmetric homodimer by pairing exposed β-strands to form an intermolecular β-sheet. A crystal structure of the designed complex closely matches the computational model (rmsd = 1.0 Å). This work demonstrates that β-strand pairing can be used to computationally design new interactions with high accuracy.

PubMed: 22143762
DOI: 10.1073/PNAS.1115124108

Experimental method

X-RAY DIFFRACTION (1.09 Å)