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Crystal structure of the catalytic domain of MMP-16/MT3-MMP: Characterization of MT-MMP specific features.

Lang, R., Braun, M., Sounni, N.E., Noel, A., Frankenne, F., Foidart, J.-M., Bode, W., Maskos, K.·2004·Journal of Molecular Biology
DOI 10.1016/j.jmb.2003.12.022
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  • The MT-loop is flexible and only present in the four membrane type MMPs, but the conformation of the MT-loop is different in each membrane type MMP and in MT1-MMP complexed with or without TIMPs.

    “The MT-loop is flexible and only present in the four membrane type MMPs, but the conformation of the MT-loop is different in each membrane type MMP (61) and in MT1-MMP complexed with or without TIMPs (62–64).”

    From Identification of amino acid residues in the MT-loop of MT1-MMP critical for its ability to cleave low-density lipoprotein receptor (2022) · cites this paper as [61]

    The retrieved passages are reference-list entries and repository metadata, not the paper’s discussion of MT-loop structure. Searches for MT-loop flexibility, its presence in four membrane-type MMPs, and differing conformations found no passage in our copy that establishes the part attributed to citation (61). The separate claim about MT1-MMP with or without TIMPs is attached to citations (62–64), not this source. (LLM, conf=0.70)

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  • Weaver et al. reported that the MT-loop, together with the hemopexin domain, is required for the translocation of MT1-MMP from the apical to the basal membrane in polarized epithelial cells during tubulogenesis, but deletion of the entire MT-loop has no significant effect on the expression, trafficking, processing, or the proteolytic activity of MT1-MMP.

    “Weaver et al. reported that the MT-loop, together with the hemopexin domain, is required for the translocation of MT1-MMP from the apical to the basal membrane in polarized epithelial cells during tubulogenesis (65), but deletion of the entire MT-loop has no significant effect on the expression, trafficking, processing, or the proteolytic activity of MT1-MMP (61, 66).”

    From Identification of amino acid residues in the MT-loop of MT1-MMP critical for its ability to cleave low-density lipoprotein receptor (2022) · cites this paper as [61]

    Split into 2 atoms — 0 confirmed, 0 partially supported, 0 disputed, 0 misattributed, 2 unverifiable. Expand the claim to see per-atom verdicts.

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Metadata

Authors
Lang, R., Braun, M., Sounni, N. E., Noel, A., Frankenne, F., Foidart, J.-M., Bode, W., & Maskos, K.
Venue
Journal of Molecular Biology
Publisher
Elsevier BV
Published
2004-02
Volume
336
Issue
1
Pages
213-225
ISSN
0022-2836
DOI
10.1016/j.jmb.2003.12.022
Cited by
42
References
0
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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