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.
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2673
2676
I. Bertini; V. Calderone; M. Fragai; C. Luchinat; S. Mangani; B. Terni
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2158/354810
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