Matrix metallopeptidase 13

1EUB, 1FLS, 1FM1, 1PEX, 1XUC, 1XUD, 1XUR, 1YOU, 1ZTQ, 2D1N, 2E2D, 2OW9, 2OZR, 2PJT, 2YIG, 3ELM, 3I7G, 3I7I, 3KEC, 3KEJ, 3KEK, 3KRY, 3LJZ, 3O2X, 3TVC, 3WV1, 3WV2, 3WV3, 3ZXH, 456C, 4A7B, 4FU4, 4FVL, 4G0D, 4JP4, 4JPA, 4L19, 5BOT, 5BOY, 5BPA, 830C432217386ENSG00000137745ENSMUSG00000050578P45452P33435NM_002427NM_008607NP_002418NP_032633Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene. It is a member of the matrix metalloproteinase (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain PDB: 1PEX​. Although the actual mechanism has not been described, the hemopexin domain participates in collagen degradation, the catalytic domain alone being particularly inefficient in collagen degradation. During embryonic development, MMP13 is expressed in the skeleton as required for restructuring the collagen matrix for bone mineralization. In pathological situations it is highly overexpressed; this occurs in human carcinomas, rheumatoid arthritis and osteoarthritis.1cxv: STRUCTURE OF RECOMBINANT MOUSE COLLAGENASE-3 (MMP-13)1eub: SOLUTION STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN COLLAGENASE-3 (MMP-13) COMPLEXED TO A POTENT NON-PEPTIDIC SULFONAMIDE INHIBITOR1fls: SOLUTION STRUCTURE OF THE CATALYTIC FRAGMENT OF HUMAN COLLAGENASE-3 (MMP-13) COMPLEXED WITH A HYDROXAMIC ACID INHIBITOR1fm1: SOLUTION STRUCTURE OF THE CATALYTIC FRAGMENT OF HUMAN COLLAGENASE-3 (MMP-13) COMPLEXED WITH A HYDROXAMIC ACID INHIBITOR1pex: COLLAGENASE-3 (MMP-13) C-TERMINAL HEMOPEXIN-LIKE DOMAIN1xuc: Matrix metalloproteinase-13 complexed with non-zinc binding inhibitor1xud: Matrix metalloproteinase-13 complexed with non-zinc binding inhibitor1xur: Matrix metalloproteinase-13 complexed with non-zinc binding inhibitor1you: Crystal structure of the catalytic domain of MMP-13 complexed with a potent pyrimidinetrione inhibitor1ztq: Crystal structure of the catalytic domain of MMP-13 complexed with WAY-0332d1n: Collagenase-3 (MMP-13) complexed to a hydroxamic acid inhibitor2e2d: Flexibility and variability of TIMP binding: X-ray structure of the complex between collagenase-3/MMP-13 and TIMP-22ow9: Crystal structure analysis of the MMP13 catalytic domain in complex with specific inhibitor456c: CRYSTAL STRUCTURE OF COLLAGENASE-3 (MMP-13) COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID830c: COLLAGENASE-3 (MMP-13) COMPLEXED TO A SULPHONE-BASED HYDROXAMIC ACID Collagenase 3 is an enzyme that in humans is encoded by the MMP13 gene. It is a member of the matrix metalloproteinase (MMP) family. Like most MMPs, it is secreted as an inactive pro-form. It is activated once the pro-domain is cleaved, leaving an active enzyme composed of the catalytic domain and the hemopexin-like domain PDB: 1PEX​. Although the actual mechanism has not been described, the hemopexin domain participates in collagen degradation, the catalytic domain alone being particularly inefficient in collagen degradation. During embryonic development, MMP13 is expressed in the skeleton as required for restructuring the collagen matrix for bone mineralization. In pathological situations it is highly overexpressed; this occurs in human carcinomas, rheumatoid arthritis and osteoarthritis. Proteins of the matrix metalloproteinase (MMP) family are involved in the breakdown of extracellular matrix in normal physiological processes, such as embryonic development, reproduction, and tissue remodeling, as well as in disease processes, such as arthritis and metastasis. Most MMPs are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The protein encoded by this gene cleaves type II collagen more efficiently than types I and III. It may be involved in articular cartilage turnover and cartilage pathophysiology associated with osteoarthritis. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.