The structural basis of CEACAM-receptor targeting by neisserial Opa proteins.
Billker
O
O
Max-Planck-Institut für Infektionsbiologie, Abteilung Molekulare Biologie, Monbijoustrasse 2, 10117 Berlin, Germany.
Popp
A
A
Gray-Owen
S D
SD
Meyer
T F
TF
D000251:Adenosine Triphosphatases / Q000737:chemistry* / Q000378:metabolism; D000942:Antigens, Bacterial / Q000235:genetics / Q000378:metabolism*; D015703:Antigens, CD / Q000378:metabolism; D000943:Antigens, Differentiation / Q000378:metabolism; D001425:Bacterial Outer Membrane Proteins / Q000737:chemistry* / Q000378:metabolism; D001665:Binding Sites; D015815:Cell Adhesion Molecules / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009343:Neisseria; D017434:Protein Structure, Tertiary
D000942:Antigens, Bacterial; D015703:Antigens, CD; D000943:Antigens, Differentiation; D001425:Bacterial Outer Membrane Proteins; C069847:CD66 antigens; D015815:Cell Adhesion Molecules; C050308:opacity proteins; D000251:Adenosine Triphosphatases