Crystal structure related to rheumatic autoimmune diseases

James Sacchettini group (Texas A&M University)


James Sacchettini's laboratory at Texas A&M University recently solved several structures, including the structure of Rsr, an ortholog of the antigenic Ro protein. Ro proteins are a class of antigenic ribonucleo-proteins associated with rheumatic autoimmune diseases in humans. Ro is suggested to play a role in RNA quality control and has also been implicated in cell survival following UV damage. The 1.9-Å crystal structure of this prokaryotic ortholog, Rsr from D. raiodurans, was determined using GM/CA-CAT beamtime. It is composed of an N-terminal domain consisting of 18 α-helices and a C-terminal domain of a β-sheet (blue) sandwiched between sets of helices. Residues in the C-terminal domain coordinate a calcium ion (yellow).

Figure: 1.9-Å crystal structure of D. radiodurans Rsr.


Ramesh, A, Savva, CG, Holzenburg, A, Sacchettini, JC. Crystal Structure of Rsr, an Ortholog of the Antigenic Ro Protein, Links Conformational Flexibility to RNA Binding Activity, J. Biol. Chem. 282 (20), 14960-14967 (2007). DOI: 10.1074/jbc.M611163200.



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