1A7B

ENGINEERING A MISFOLDED FORM OF CD2

Summary for 1A7B

• Entry DOI: 10.2210/pdb1a7b/pdb
• Descriptor: CD2 (1 entity in total)
• Functional Keywords: cd2, domain swapping, oligomerization, protein folding, protein evolution
• Biological source: Rattus norvegicus (Norway rat)
• Cellular location: Membrane; Single-pass type I membrane protein: P08921
• Total number of polymer chains: 4
• Total formula weight: 43593.04

Authors

Murray, A.J.,Head, J.G.,Barker, J.J.,Brady, R.L. (deposition date: 1998-03-10, release date: 1998-06-17, Last modification date: 2024-05-22)

Primary citation

Murray, A.J.,Head, J.G.,Barker, J.J.,Brady, R.L.
Engineering an intertwined form of CD2 for stability and assembly.
Nat.Struct.Biol., 5:778-782, 1998

PubMed Abstract: The amino-terminal domain of CD2 has the remarkable ability to fold in two ways: either as a monomer or as an intertwined, metastable dimer. Here we show that it is possible to differentially stabilize either fold by engineering the CD2 sequence, mimicking random mutagenesis events that could occur during molecular evolution. Crystal structures of a hinge-deletion mutant, which is stable as an intertwined dimer, reveal domain rotations that enable the protein to further assemble to a tetramer. These results demonstrate that a variety of folds can be adopted by a single polypeptide sequence, and provide guidance for the design of proteins capable of further assembly.

PubMed: 9731771
DOI: 10.1038/1816

Experimental method

X-RAY DIFFRACTION (3.1 Å)