Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.
Kochan, Grazyna
Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America May 2011 - 7745-50 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1091-6490
10.1073/pnas.1101262108 doi
Amino Acid Sequence
Amino Acid Substitution
Aminopeptidases--chemistry
Antigen Presentation
Catalytic Domain--genetics
Crystallography, X-Ray
HLA-B27 Antigen--metabolism
Humans
Minor Histocompatibility Antigens
Models, Molecular
Mutagenesis, Site-Directed
Polymorphism, Single Nucleotide
Protein Conformation
Protein Processing, Post-Translational
Protein Structure, Tertiary
Recombinant Proteins--chemistry
Spondylitis, Ankylosing--enzymology
Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming. [electronic resource] - Proceedings of the National Academy of Sciences of the United States of America May 2011 - 7745-50 p. digital
Publication Type: Journal Article; Research Support, Non-U.S. Gov't
1091-6490
10.1073/pnas.1101262108 doi
Amino Acid Sequence
Amino Acid Substitution
Aminopeptidases--chemistry
Antigen Presentation
Catalytic Domain--genetics
Crystallography, X-Ray
HLA-B27 Antigen--metabolism
Humans
Minor Histocompatibility Antigens
Models, Molecular
Mutagenesis, Site-Directed
Polymorphism, Single Nucleotide
Protein Conformation
Protein Processing, Post-Translational
Protein Structure, Tertiary
Recombinant Proteins--chemistry
Spondylitis, Ankylosing--enzymology