It has been shown to cleave laminin 5 and is localized in the basal epithelial layer of bovine skin.
The BMP1 locus encodes a protein that is capable of inducing formation of cartilage in vivo. Although other bone morphogenetic proteins are members of the TGF-beta superfamily, BMP1 encodes a protein that is not closely related to other known growth factors. BMP1 protein and procollagen C proteinase (PCP), a secreted metalloprotease requiring calcium and needed for cartilage and bone formation, are identical. PCP or BMP1 protein cleaves the C-terminal propeptides of procollagen I, II, and III and its activity is increased by the procollagen C-endopeptidase enhancer protein. The BMP1 gene is expressed as alternatively spliced variants that share an N-terminal protease domain but differ in their C-terminal region
The structure of BMP1 was determined through X-Ray diffraction with a resolution of 1.27 Å. Crystallization experiments were done by vapor diffusion at a pH of 7.5. This is important because it is close to the pH of the human body, where BMP1 resides in vivo. BMP1 is 202 residues in length. Its secondary structure is made up of 30% helices, or 10 helices, 61 residues in length, and 15% beta sheets, or 11 strands, 32 residues in length. It contains ligands of an acetyl group and a Zinc ion.
A Ramachandran plot was constructed for BMP. This plot shows that BMP1 most prefers Phi and Psi angles (Phi, Psi) of around (-60°,-45°) and (-60°, 140°). These preferred angles are an estimate of the most clustered data of the Ramachandran plot. The preferred region is much greater in range. 97% of the residues were in preferred regions and 100% of the residues were in the allowed region, with no outliers.
^Tabas JA, Zasloff M, Wasmuth JJ, Emanuel BS, Altherr MR, McPherson JD, Wozney JM, Kaplan FS (February 1991). "Bone morphogenetic protein: chromosomal localization of human genes for BMP1, BMP2A, and BMP3". Genomics9 (2): 283–9. doi:10.1016/0888-7543(91)90254-C. PMID2004778.
^PDB3EDG; Mac Sweeney A, Gil-Parrado S, Vinzenz D, Bernardi A, Hein A, Bodendorf U, Erbel P, Logel C, Gerhartz B (December 2008). "Structural basis for the substrate specificity of bone morphogenetic protein 1/tolloid-like metalloproteases". J. Mol. Biol.384 (1): 228–39. doi:10.1016/j.jmb.2008.09.029. PMID18824173.
Tabas JA, Zasloff M, Wasmuth JJ, et al. (1991). "Bone morphogenetic protein: chromosomal localization of human genes for BMP1, BMP2A, and BMP3.". Genomics9 (2): 283–9. doi:10.1016/0888-7543(91)90254-C. PMID2004778.
Wozney JM, Rosen V, Celeste AJ, et al. (1989). "Novel regulators of bone formation: molecular clones and activities.". Science242 (4885): 1528–34. doi:10.1126/science.3201241. PMID3201241.
Takahara K, Lyons GE, Greenspan DS (1995). "Bone morphogenetic protein-1 and a mammalian tolloid homologue (mTld) are encoded by alternatively spliced transcripts which are differentially expressed in some tissues.". J. Biol. Chem.269 (51): 32572–8. PMID7798260.
Yoshiura K, Tamura T, Hong HS, et al. (1993). "Mapping of the bone morphogenetic protein 1 gene (BMP1) to 8p21: removal of BMP1 from candidacy for the bone disorder in Langer-Giedion syndrome.". Cytogenet. Cell Genet.64 (3–4): 208–9. doi:10.1159/000133577. PMID8404039.
Takahara K, Lee S, Wood S, Greenspan DS (1996). "Structural organization and genetic localization of the human bone morphogenetic protein 1/mammalian tolloid gene". Genomics29 (1): 9–15. doi:10.1006/geno.1995.1209. PMID8530106.
Janitz M, Heiser V, Böttcher U, et al. (1998). "Three alternatively spliced variants of the gene coding for the human bone morphogenetic protein-1". J. Mol. Med.76 (2): 141–6. doi:10.1007/s001090050202. PMID9500680.
Scott IC, Blitz IL, Pappano WN, et al. (1999). "Mammalian BMP-1/Tolloid-related metalloproteinases, including novel family member mammalian Tolloid-like 2, have differential enzymatic activities and distributions of expression relevant to patterning and skeletogenesis". Dev. Biol.213 (2): 283–300. doi:10.1006/dbio.1999.9383. PMID10479448.
Amano S, Scott IC, Takahara K, et al. (2000). "Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain". J. Biol. Chem.275 (30): 22728–35. doi:10.1074/jbc.M002345200. PMID10806203.
Scott IC, Blitz IL, Pappano WN, et al. (2001). "Homologues of Twisted gastrulation are extracellular cofactors in antagonism of BMP signalling". Nature410 (6827): 475–8. doi:10.1038/35068572. PMID11260715.
Garrigue-Antar L, Barker C, Kadler KE (2001). "Identification of amino acid residues in bone morphogenetic protein-1 important for procollagen C-proteinase activity". J. Biol. Chem.276 (28): 26237–42. doi:10.1074/jbc.M010814200. PMID11283002.
Unsöld C, Pappano WN, Imamura Y, et al. (2002). "Biosynthetic processing of the pro-alpha 1(V)2pro-alpha 2(V) collagen heterotrimer by bone morphogenetic protein-1 and furin-like proprotein convertases". J. Biol. Chem.277 (7): 5596–602. doi:10.1074/jbc.M110003200. PMID11741999.
Rattenholl A, Pappano WN, Koch M, et al. (2002). "Proteinases of the bone morphogenetic protein-1 family convert procollagen VII to mature anchoring fibril collagen". J. Biol. Chem.277 (29): 26372–8. doi:10.1074/jbc.M203247200. PMID11986329.
Garrigue-Antar L, Hartigan N, Kadler KE (2003). "Post-translational modification of bone morphogenetic protein-1 is required for secretion and stability of the protein". J. Biol. Chem.277 (45): 43327–34. doi:10.1074/jbc.M207342200. PMID12218058.
Hartigan N, Garrigue-Antar L, Kadler KE (2003). "Bone morphogenetic protein-1 (BMP-1). Identification of the minimal domain structure for procollagen C-proteinase activity". J. Biol. Chem.278 (20): 18045–9. doi:10.1074/jbc.M211448200. PMID12637537.
Leighton M, Kadler KE (2003). "Paired basic/Furin-like proprotein convertase cleavage of Pro-BMP-1 in the trans-Golgi network". J. Biol. Chem.278 (20): 18478–84. doi:10.1074/jbc.M213021200. PMID12637569.
Ota T, Suzuki Y, Nishikawa T, et al. (2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nat. Genet.36 (1): 40–5. doi:10.1038/ng1285. PMID14702039.