Cited by 90Protease and Inhibitor MechanismsEnzyme Structure and FunctionProtein Structure and Dynamics

Crystal Structure of the Catalytic Domain of Human ADAM33

Orth, Peter, Reichert, Paul, Wang, Wenyan, Prosise, Winifred W., Yarosh-Tomaine, Taisa, Hammond, Gerald, Ingram, Richard N., Xiao, Li +6 more·2004·Journal of Molecular Biology

Abstract

Adam33 is a putative asthma susceptibility gene encoding for a membrane-anchored metalloprotease belonging to the ADAM family. The ADAMs (a disintegrin and metalloprotease) are a family of glycoproteins implicated in cell-cell interactions, cell fusion, and cell signaling. We have determined the crystal structure of the Adam33 catalytic domain in complex with the inhibitor marimastat and the inhibitor-free form. The structures reveal the polypeptide fold and active site environment resembling that of other metalloproteases. The substrate-binding site contains unique features that allow the structure-based design of specific inhibitors of this enzyme.

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Crossref · 10.1016/j.jmb.2003.10.037

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  • Ntn superfamily members with structures similar to the RoseTTAFold model suggest that TANGO2 functions as an enzyme that might hydrolyze a carbon-nitrogen bond in a membrane component.

    “Ntn superfamily members with structures similar to the RoseTTAFold model suggest that TANGO2 functions as an enzyme that might hydrolyze a carbon-nitrogen bond in a membrane component (18).”

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Authors
Orth, P., Reichert, P., Wang, W., Prosise, W. W., Yarosh-Tomaine, T., Hammond, G., Ingram, R. N., Xiao, L., Mirza, U. A., Zou, J., Strickland, C., Taremi, S. S., Le, H. V., & Madison, V.
Corresponding author
Orth, Peter
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2004-01
Volume
335
Issue
1
Pages
129-137
ISSN
0022-2836 (ISSN-L)
OpenAlex
W2115301251
Cited by
90
References
23
Citations by year
2026: 1 · 2025: 2 · 2024: 2 · 2023: 1 · 2022: 2 · 2021: 1 · 2020: 2 · 2019: 4 · 2018: 3 · 2017: 5 · 2016: 4 · 2015: 1 · 2013: 2 · 2012: 6
FWCI
2.86
Type
journal article
Language
en
Open access
closed
Locations
  • Journal of Molecular Biology (publishedVersion)
  • PubMed (publishedVersion)
Funders
Basic Energy Sciences
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
Keywords
ADAM33, catalytic domain, crystal structure, metalloproteinases, marimastat, asthma susceptibility genes, ADAM family, substrate binding site, active site, enzyme inhibitor design, structure-based drug design
MeSH terms
Amino Acid Sequence, Enzyme Inhibitors, Humans, Hydroxamic Acids, Metalloendopeptidases, Models, Molecular, Mutation, Protein Binding, Molecular Structure, Sequence Alignment, Protein Structure, Tertiary, Crystallography, X-Ray, Catalytic Domain, ADAM Proteins

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