Int. J. Mol. Sci., Volume 20, Issue 17 (September-1 2019) – 253 articles
Cover Story (view full-size image): The extracellular matrix metalloproteinase-2 (MMP-2) is associated with several important disease processes. The molecular dynamics of MMP-2 with its associated metal ions (Zn2+ and Ca2+) were analyzed. Inter-domain motions affecting the orientation of the Hpx domain in relation to the Cat and Fib domains are facilitated by the linker region. The catalytic Zn2+ ion and Ca2+ ion that stabilizes the relationship between the Cat and Fib domains are tightly bound within their defined pockets. The Zn2+ associated with the S-loop demonstrates increased flexibility. The remaining Ca2+ ions play minimal roles in conformational stability. The detailed conformational analysis provides the possibility of structure-based inhibitor design. View this paper.
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