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 NH3+ ion is either triply hydrogen bonded, or only exhibits van der Waals interactions.
X-ray structures of binary and ternary enzyme-product-Inhibitor complexes of matrix metalloproteinases / I. Bertini; V. Calderone; M. Fragai; C. Luchinat; S. Mangani; B. Terni. - In: ANGEWANDTE CHEMIE. INTERNATIONAL EDITION. - ISSN 1433-7851. - STAMPA. - 42:(2003), pp. 2673-2676. [10.1002/anie.200350957]
X-ray structures of binary and ternary enzyme-product-Inhibitor complexes of matrix metalloproteinases
BERTINI, IVANO;CALDERONE, VITO;FRAGAI, MARCO;LUCHINAT, CLAUDIO;
2003
Abstract
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 NH3+ ion is either triply hydrogen bonded, or only exhibits van der Waals interactions.File | Dimensione | Formato | |
---|---|---|---|
MMP12_ternary.pdf
Accesso chiuso
Tipologia:
Pdf editoriale (Version of record)
Licenza:
Tutti i diritti riservati
Dimensione
142.12 kB
Formato
Adobe PDF
|
142.12 kB | Adobe PDF | Richiedi una copia |
I documenti in FLORE sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.