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.
Bertini, I., Calderone, V., Fragai, M., Luchinat, C., Mangani, S., Terni, B. (2003). X-ray structures of ternary enzyme-product-inhibitor complexes of MMP. ANGEWANDTE CHEMIE. INTERNATIONAL EDITION, 42(23), 2673-2676 [10.1002/anie.200350957].
X-ray structures of ternary enzyme-product-inhibitor complexes of MMP
Mangani, Stefano;
2003-01-01
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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https://hdl.handle.net/11365/32114
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