Catalytic domain of MMP20 (Enamelysin) - the NMR structure of a new matrix metalloproteinase.
The solution structure of the catalytic domain of MMP-20, a member of the matrix metalloproteinases family not yet structurally characterized, complexed with N-Isobutyl-N-(4-methoxyphenylsulfonyl)glycyl hydroxamic acid (NNGH), is here reported and compared with other MMPs-NNGH adducts. The backbone dynamic has been characterized as well. We have found that, despite the same fold and very high overall similarity, the present structure experiences specific structural and dynamical similarities with some MMPs and differences with others, around the catalytic cavity. The present solution structure, not only contributes to fill the gap of structural knowledge on human MMPs, but also provides further information to design more selective and efficient inhibitors for a specific member of this class of proteins.
Arendt
Yvonne
Y
ProtEra S.r.l., Via delle Idee 22, 50019 Sesto Fiorentino (FI), Italy.
Banci
Lucia
L
Bertini
Ivano
I
Cantini
Francesca
F
Cozzi
Roberta
R
Del Conte
Rebecca
R
Gonnelli
Leonardo
L
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D017124:Conserved Sequence; D053519:Matrix Metalloproteinase 20 / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D011485:Protein Binding; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D040681:Structural Homology, Protein
D053519:Matrix Metalloproteinase 20