Summary
PDB 2X44 deposited: 2010-01-28 modified: 2011-08-10
Title STRUCTURE OF A STRAND-SWAPPED DIMERIC FORM OF CTLA-4
Authors Davis, S.J., Evans, E.J., Gilbert, R.J.C., Sonnen, A.F., Stuart, D.I., Yu, C.
Method X-RAY DIFFRACTION
Structure factors resolution 2.6 rfactor 0.19157 rfree 0.24501
DPI 1.00 theoretical min: 0.38
Citations

We present the crystal structure of an immunoglobulin light-chain-like domain, CTLA-4, as a strand-swapped dimer displaying cis-trans proline isomerisation and native-like hydrogen bonding. We also show that CTLA-4 can form amyloid-like fibres and amorphous deposits explainable by the same strand swapping. Our results suggest a molecular basis for the pathological aggregation of immunoglobulin domains and why amyloid-like fibres are more often composed of homologous rather than heterologous subunits.

J.Mol.Biol. 2010 Jun; 399(2):207- doi:10.1016/J.JMB.2010.04.011

Cross References
Database source Identifier Description
PubMed 20394753 JMOBAK
Biomolecule Structure Assembly Serial Assembly Type Conformational State Chains Ligands Atoms
2X44/1 2X44 1 dimer 0 2 0 1888