Structural insights into the CFTR-NHERF interaction.
Ladias
J A A
JA
Molecular Medicine Laboratory and Macromolecular Crystallography Unit, Division of Experimental Medicine, Harvard Institutes of Medicine, Harvard Medical School, 4 Blackfan Circle, Boston, MA 02115, USA. jladias@caregroup.harvard.edu
D000818:Animals; D001120:Arginine / Q000737:chemistry; D001665:Binding Sites; D003461:Crystallography / Q000379:methods; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D006706:Homeostasis / Q000502:physiology; D006801:Humans; D015640:Ion Channel Gating / Q000502:physiology; D046911:Macromolecular Substances; D008958:Models, Molecular; D010750:Phosphoproteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D011485:Protein Binding; D011487:Protein Conformation; D017434:Protein Structure, Tertiary; D017923:Sodium-Hydrogen Exchangers; D013329:Structure-Activity Relationship
C505032:CFTR protein, human; D046911:Macromolecular Substances; D010750:Phosphoproteins; D017923:Sodium-Hydrogen Exchangers; C093376:sodium-hydrogen exchanger regulatory factor; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D001120:Arginine