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X‐ray Structures of Binary and Ternary Enzyme‐Product‐Inhibitor Complexes of Matrix Metalloproteinases
Author(s) -
Bertini Ivano,
Calderone Vito,
Fragai Marco,
Luchinat Claudio,
Mangani Stefano,
Terni Beatrice
Publication year - 2003
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200350957
Subject(s) - van der waals force , ternary operation , cleavage (geology) , crystallography , chemistry , catalysis , molecule , yield (engineering) , product (mathematics) , stereochemistry , protein filament , physics , materials science , biochemistry , computer science , mathematics , organic chemistry , thermodynamics , fracture (geology) , composite material , programming language , geometry
A helicoidal filament results from the approach of the N‐terminus of the mutated variant of the catalytic domain of MMP‐12 with the catalytic zinc center of another molecule (see X‐ray structure); adjacent filaments are arranged in double helices. The N‐terminal fragment is proposed to be analogous to an N‐terminal polypeptide product after cleavage. Crystals yield two contrasting structures, in which the NH 3 + ion is either triply hydrogen bonded, or only exhibits van der Waals interactions.