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Literature summary for 3.5.3.15 extracted from

  • Saijo, S.; Nagai, A.; Kinjo, S.; Mashimo, R.; Akimoto, M.; Kizawa, K.; Yabe-Wada, T.; Shimizu, N.; Takahara, H.; Unno, M.
    Monomeric form of peptidylarginine deiminase type I revealed by X-ray crystallography and small-angle X-ray scattering (2016), J. Mol. Biol., 428, 3058-3073 .
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
structure of isoform Pad1, in presence of Ca2+, to 3.2 A resolution. The asymmetric unit containes two PAD1 molecules, with an elongated N-terminal loop that appears to prevent the formation of a homodimer. The N-terminal loop occupies the substrate binding site of the adjacent PAD1 molecules in the crystal Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens Q9ULC6 isoform PAD1
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Synonyms

Synonyms Comment Organism
PAD1
-
Homo sapiens
PADI1
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Homo sapiens