Sequence analysis suggests the presence of an IG-like domain in the N-terminal region of α-dystroglycan which was crystallized after mutation of a protease susceptible site (Arg168→His)

Matrix Biology

Volumn 17, Issue 7, 1998, Pages 495-500

  Bozic, Damir ^a   Engel, Jürgen ^a   Brancaccio, Andrea ^b,c  

^a UNIVERSITY OF BASEL   (Switzerland)

^b CNR   (Italy)

^c CATHOLIC UNIVERSITY   (Italy)

Author keywords

Immunoglobulins; Mutagenesis; Protein crystallography; Sequence analysis; dystroglycan

Indexed keywords

DYSTROGLYCAN; GLOBULAR PROTEIN; IMMUNOGLOBULIN; MUTANT PROTEIN; PROTEINASE; RECOMBINANT PROTEIN; THROMBIN;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CRYSTALLOGRAPHY; GENE MUTATION; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN PURIFICATION; SEQUENCE ANALYSIS; X RAY DIFFRACTION;

ANIMALIA; BACTERIA (MICROORGANISMS);

EID: 0031697295     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(98)90097-X     Document Type: Article

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