Structural basis for Ca(2+)-induced activation of human PAD4
Structural basis for Ca(2+)-induced activation of human PAD4
About this item
Full title
Structural basis for Ca(2+)-induced activation of human PAD4
Author / Creator
Publisher
United States
Journal title
Nature structural & molecular biology, 2004-08, Vol.11 (8), p.777
Language
English
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Publication information
Publisher
United States
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Scope and Contents
Contents
Peptidylarginine deiminase 4 (PAD4) is a Ca(2+)-dependent enzyme that catalyzes the conversion of protein arginine residues to citrulline. Its gene is a susceptibility locus for rheumatoid arthritis. Here we present the crystal structure of Ca(2+)-free wild-type PAD4, which shows that the polypeptide chain adopts an elongated fold in which the N-te...
Alternative Titles
Full title
Structural basis for Ca(2+)-induced activation of human PAD4
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Record Identifier
TN_cdi_pubmed_primary_15247907
Permalink
https://devfeature-collection.sl.nsw.gov.au/record/TN_cdi_pubmed_primary_15247907
Other Identifiers
ISSN
1545-9993
DOI
10.1038/nsmb799
