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PDBsum entry 2clt
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References listed in PDB file
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Key reference
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Title
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Crystal structure of an active form of human mmp-1.
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Authors
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S.Iyer,
R.Visse,
H.Nagase,
K.R.Acharya.
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Ref.
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J Mol Biol, 2006,
362,
78-88.
[DOI no: ]
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PubMed id
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Abstract
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The extracellular matrix is a dynamic environment that constantly undergoes
remodelling and degradation during vital physiological processes such as
angiogenesis, wound healing, and development. Unbalanced extracellular matrix
breakdown is associated with many diseases such as arthritis, cancer and
fibrosis. Interstitial collagen is degraded by matrix metalloproteinases with
collagenolytic activity by MMP-1, MMP-8 and MMP-13, collectively known as the
collagenases. Matrix metalloproteinase 1 (MMP-1) plays a pivotal role in
degradation of interstitial collagen types I, II, and III. Here, we report the
crystal structure of the active form of human MMP-1 at 2.67 A resolution. This
is the first MMP-1 structure that is free of inhibitor and a water molecule
essential for peptide hydrolysis is observed coordinated with the active site
zinc. Comparing this structure with the human proMMP-1 shows significant
structural differences, mainly in the relative orientation of the hemopexin
domain, between the pro form and active form of the human enzyme.
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Figure 3.
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Figure 4.
Figure 4. Comparison of the hydrogen-bonding interactions
within the linker region. (a) Superposition of active MMP-1
(pink) and procollagenase-1 (green) to highlight the
conformational similarity of the linker region in the two
structures. (b) Stereo view of the linker region in active MMP-1
showing the hydrogen-bonding interactions between the residues.
(c) Stereo view of the linker region in procollagenase-1 showing
the hydrogen bonds within the region.
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The above figures are
reprinted
from an Open Access publication published by Elsevier:
J Mol Biol
(2006,
362,
78-88)
copyright 2006.
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