Modelling the human rhesus proteins: Implications for structure and function

British Journal of Haematology

Volumn 131, Issue 4, 2005, Pages 543-551

  Conroy, Matthew J ^b   Bullough, Per A ^b   Merrick, Mike ^c   Avent, Neil D ^a  

^a UNIVERSITY OF THE WEST OF ENGLAND   (United Kingdom)

^b UNIVERSITY OF SHEFFIELD   (United Kingdom)

^c JOHN INNES CENTRE   (United Kingdom)

Author keywords

Ammonium transport; Homology model; Membrane complex; Oligomeric state; Rhesus protein

Indexed keywords

AMMONIUM CHANNEL B PROTEIN; OLIGOMER; PROTEIN; RHESUS ANTIGEN; RHESUS D ANTIGEN; UNCLASSIFIED DRUG; AMTB PROTEIN, E COLI; CATION TRANSPORT PROTEIN; ESCHERICHIA COLI PROTEIN; QUATERNARY AMMONIUM DERIVATIVE;

ALGORITHM; AMINO ACID SEQUENCE; ARTICLE; CRYSTAL STRUCTURE; ESCHERICHIA COLI; MODEL; OLIGOMERIZATION; PREDICTION; PRIORITY JOURNAL; PROTEIN FAMILY; PROTEIN FUNCTION; PROTEIN GLYCOSYLATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY; BLOOD GROUP RHESUS SYSTEM; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; MOLECULAR GENETICS; PROTEIN CONFORMATION; STRUCTURE ACTIVITY RELATION; X RAY CRYSTALLOGRAPHY;

AMINO ACID SEQUENCE; CATION TRANSPORT PROTEINS; CRYSTALLOGRAPHY, X-RAY; ESCHERICHIA COLI PROTEINS; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; QUATERNARY AMMONIUM COMPOUNDS; RH-HR BLOOD-GROUP SYSTEM; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 33644803306     PISSN: 00071048     EISSN: 13652141     Source Type: Journal    
DOI: 10.1111/j.1365-2141.2005.05786.x     Document Type: Article

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