1f0v
From Proteopedia
Crystal structure of an Rnase A dimer displaying a new type of 3D domain swapping
Overview
Bovine pancreatic ribonuclease (RNase A) forms two types of dimers (a major and a minor component) upon concentration in mild acid. These two dimers exhibit different biophysical and biochemical properties. Earlier we reported that the minor dimer forms by swapping its N-terminal alpha-helix with that of an identical molecule. Here we find that the major dimer forms by swapping its C-terminal beta-strand, thus revealing the first example of three-dimensional (3D) domain swapping taking place in different parts of the same protein. This feature permits RNase A to form tightly bonded higher oligomers. The hinge loop of the major dimer, connecting the swapped beta-strand to the protein core, resembles a short segment of the polar zipper proposed by Perutz and suggests a model for aggregate formation by 3D domain swapping with a polar zipper.
About this Structure
1F0V is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
Reference
A domain-swapped RNase A dimer with implications for amyloid formation., Liu Y, Gotte G, Libonati M, Eisenberg D, Nat Struct Biol. 2001 Mar;8(3):211-4. PMID:11224563 Page seeded by OCA on Wed Apr 30 13:52:58 2008
