Brangulis, Kalvis <br/><br/>
Crystal structures of the Erp protein family members ErpP and ErpC from Borrelia burgdorferi reveal the reason for different affinities for complement regulator factor H.  [electronic resource] 

 -  Biochimica et biophysica acta  May 2015 
 - 349-55 p.  digital 
<br/><br/> Publication Type: Comparative Study; Journal Article; Research Support, Non-U.S. Gov't 
<br/><br/><label>ISSN: </label>0006-3002 
<br/><br/><label>Standard No.: </label>10.1016/j.bbapap.2014.12.025  doi 
<br/><br/><label>Subjects--Topical Terms: </label><br/>Amino Acid Sequence<br/>Bacterial Outer Membrane Proteins--chemistry<br/>Binding Sites<br/>Complement Factor H--metabolism<br/>Crystallography, X-Ray<br/>Models, Molecular<br/>Molecular Sequence Data<br/>Protein Binding<br/>Protein Structure, Secondary<br/>Protein Structure, Tertiary<br/>Receptors, Cell Surface--chemistry<br/>Sequence Homology, Amino Acid<br/>Substrate Specificity