title: Matrix metalloproteinase interactions with collagen and elastin.
abstract: Most abundant in the extracellular matrix are collagens, joined by elastin that confers elastic recoil to the lung, aorta, and skin. These fibrils are highly resistant to proteolysis but can succumb to a minority of the matrix metalloproteinases (MMPs). Considerable inroads to understanding how such MMPs move to the susceptible sites in collagen and then unwind the triple helix of collagen monomers have been gained. The essential role in unwinding of the hemopexin-like domain of interstitial collagenases or the collagen binding domain of gelatinases is highlighted. Elastolysis is also facilitated by the collagen binding domain in the cases of MMP-2 and MMP-9, and remote exosites of the catalytic domain in the case of MMP-12.
authors.affiliation: Department of Biochemistry, University of Missouri, 117 Schweitzer Hall, Columbia, MO 65211, USA. Electronic address: vandorens@missouri.edu.
authors.forename: Steven R
authors.initials: SR
authors.lastname: Van Doren
mesh_terms: D001665:Binding Sites; D003094:Collagen / Q000737:chemistry / Q000378:metabolism*; D004549:Elastin / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D020782:Matrix Metalloproteinases / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D017433:Protein Structure, Secondary; D059748:Proteolysis; D013379:Substrate Specificity
chemical_list: D003094:Collagen; D004549:Elastin; D020782:Matrix Metalloproteinases
keywords: Collagen triple helix; Elastin; Exosite; Matrix metalloproteinases