| Matrix metallopeptidase 1 (interstitial collagenase) |  | | PDB rendering based on 1ayk. | | Available structures | | 1ayk, 1cge, 1cgf, 1cgl, 1hfc, 1su3, 2ayk, 2clt, 2j0t, 2tcl, 3ayk, 4ayk, 966c | | Identifiers | | Symbols | MMP1; CLGN; CLG | | External IDs | OMIM: 120353 MGI: 1933846 HomoloGene: 20544 | | | | RNA expression pattern |  | | More reference expression data | | Orthologs | | Species | Human | Mouse | | Entrez | 4312 | 83995 | | Ensembl | ENSG00000196611 | ENSMUSG00000043089 | | UniProt | P03956 | Q149J4 | | RefSeq | NM_002421 (mRNA) | XM_001000512 (mRNA) | | NP_002412 (protein) | XP_001000512 (protein) | | Location | Chr 11:
102.17 - 102.17 Mb | Chr 9:
7.46 - 7.48 Mb | | PubMed search | [1] | [2] | Interstitial collagenase is an enzyme that in humans is encoded by the MMP1 gene. 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 MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. This gene encodes a secreted enzyme which breaks down the interstitial collagens, types I, II, and III. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.[1] In addition, mechanical force may increase the expression of MMP1 in human periodontal ligament cells.[2] [edit] Interactions MMP1 has been shown to interact with CD49b.[3][4] [edit] References - ^ "Entrez Gene: MMP1 matrix metallopeptidase 1 (interstitial collagenase)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4312.
- ^ Sheng-Fu Huang; Yu-Hong Li; Ren, Yi-jin; Zheng-Guo Cao; Xing Long (Aug 2008). "The effect of a single nucleotide polymorphism in the matrix metalloproteinase-1 (MMP-1) promoter on force-induced MMP-1 expression in human periodontal ligament cells.". Eur J Oral Sci. 116 (4): 319–23. doi:10.1111/j.1600-0722.2008.00552.x. PMID 18705799.
- ^ Stricker, T P; Dumin J A, Dickeson S K, Chung L, Nagase H, Parks W C, Santoro S A (Aug. 2001). "Structural analysis of the alpha(2) integrin I domain/procollagenase-1 (matrix metalloproteinase-1) interaction". J. Biol. Chem. (United States) 276 (31): 29375-81. doi:10.1074/jbc.M102217200. ISSN 0021-9258. PMID 11359774.
- ^ Dumin, J A; Dickeson S K, Stricker T P, Bhattacharyya-Pakrasi M, Roby J D, Santoro S A, Parks W C (Aug. 2001). "Pro-collagenase-1 (matrix metalloproteinase-1) binds the alpha(2)beta(1) integrin upon release from keratinocytes migrating on type I collagen". J. Biol. Chem. (United States) 276 (31): 29368-74. doi:10.1074/jbc.M104179200. ISSN 0021-9258. PMID 11359786.
[edit] Further reading - Krane SM (1995). "Is collagenase (matrix metalloproteinase-1) necessary for bone and other connective tissue remodeling?". Clin. Orthop. Relat. Res. (313): 47–53. PMID 7641497.
- Massova I, Kotra LP, Fridman R, Mobashery S (1998). "Matrix metalloproteinases: structures, evolution, and diversification.". Faseb J. 12 (12): 1075–95. PMID 9737711.
- Nagase H, Woessner JF (1999). "Matrix metalloproteinases.". J. Biol. Chem. 274 (31): 21491–4. doi:10.1074/jbc.274.31.21491. PMID 10419448.
- Okada Y, Hashimoto G (2002). "[Degradation of extracellular matrix by matrix metalloproteinases and joint destruction]". Seikagaku 73 (11): 1309–21. PMID 11831026.
- Seiki M (2003). "Membrane-type 1 matrix metalloproteinase: a key enzyme for tumor invasion.". Cancer Lett. 194 (1): 1–11. doi:10.1016/S0304-3835(02)00699-7. PMID 12706853.
- Golubkov VS, Strongin AY (2007). "Proteolysis-driven oncogenesis.". Cell Cycle 6 (2): 147–50. PMID 17245132.
| PDB Gallery | | | | | 1ayk: INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, 30 STRUCTURES | | | | 1cge: CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF | | | | 1cgf: CRYSTAL STRUCTURES OF RECOMBINANT 19-KDA HUMAN FIBROBLAST COLLAGENASE COMPLEXED TO ITSELF | | | | 1cgl: STRUCTURE OF THE CATALYTIC DOMAIN OF FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR | | | | 1hfc: 1.56 ANGSTROM STRUCTURE OF MATURE TRUNCATED HUMAN FIBROBLAST COLLAGENASE | | | | 1su3: X-ray structure of human proMMP-1: New insights into collagenase action | | | | 2ayk: INHIBITOR-FREE CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE, NMR, MINIMIZED AVERAGE STRUCTURE | | | | 2clt: CRYSTAL STRUCTURE OF THE ACTIVE FORM (FULL-LENGTH) OF HUMAN FIBROBLAST COLLAGENASE. | | | | 2j0t: CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF MMP-1 IN COMPLEX WITH THE INHIBITORY DOMAIN OF TIMP-1 | | | | 2tcl: STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH AN INHIBITOR | | | | 3ayk: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, MINIMIZED AVERAGE STRUCTURE | | | | 4ayk: CATALYTIC FRAGMENT OF HUMAN FIBROBLAST COLLAGENASE COMPLEXED WITH CGS-27023A, NMR, 30 STRUCTURES | | | | 966c: CRYSTAL STRUCTURE OF FIBROBLAST COLLAGENASE-1 COMPLEXED TO A DIPHENYL-ETHER SULPHONE BASED HYDROXAMIC ACID | | | | |
