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Bone morphogenetic protein 1

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Title: Bone morphogenetic protein 1  
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Bone morphogenetic protein 1

Bone morphogenetic protein 1
PDB rendering based on 3edg.
Available structures
PDB Ortholog search: PDBe, RCSB
Identifiers
Symbols  ; OI13; PCOLC; PCP; PCP2; TLD
External IDs ChEMBL: GeneCards:
EC number
RNA expression pattern
Orthologs
Species Human Mouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)
RefSeq (protein)
Location (UCSC)
PubMed search

Bone morphogenetic protein 1, also known as BMP1, is a protein which in humans is encoded by the BMP1 gene.[1][2] There are seven isoforms of the protein created by alternate splicing.

Contents

  • Function 1
  • Structure 2
  • References 3
  • Further reading 4
  • External links 5
  • External links 6

Function

BMP1 belongs to the peptidase M12A family of bone morphogenetic proteins (BMPs). It induces bone and cartilage development. Unlike other BMPs, it does not belong to the TGFβ superfamily. It was initially discovered to work like other BMPs by inducing bone and cartilage development. It however, is a metalloprotease that cleaves the C-terminus of procollagen I, II and III. It has an astacin-like protease domain.

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[1]

Structure

The structure of BMP1 was determined through X-Ray diffraction with a resolution of 1.27 Å.[3] 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 [4] 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.

References

  1. ^ a b "Entrez Gene: BMP1 bone morphogenetic protein 1". 
  2. ^ 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". Genomics 9 (2): 283–9.  
  3. ^ ​; 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.  
  4. ^ "MolProbity Ramachandran analysis of 3EDG, model 1" (PDF). www.rcsb.org. 

Further reading

  • Tabas JA, Zasloff M, Wasmuth JJ; et al. (1991). "Bone morphogenetic protein: chromosomal localization of human genes for BMP1, BMP2A, and BMP3.". Genomics 9 (2): 283–9.  
  • Wozney JM, Rosen V, Celeste AJ; et al. (1989). "Novel regulators of bone formation: molecular clones and activities.". Science 242 (4885): 1528–34.  
  • 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.  
  • 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.  
  • Takahara K, Lee S, Wood S, Greenspan DS (1996). "Structural organization and genetic localization of the human bone morphogenetic protein 1/mammalian tolloid gene". Genomics 29 (1): 9–15.  
  • Kessler E, Takahara K, Biniaminov L; et al. (1996). "Bone morphogenetic protein-1: the type I procollagen C-proteinase". Science 271 (5247): 360–2.  
  • Li SW, Sieron AL, Fertala A; et al. (1996). "The C-proteinase that processes procollagens to fibrillar collagens is identical to the protein previously identified as bone morphogenic protein-1". Proc. Natl. Acad. Sci. U.S.A. 93 (10): 5127–30.  
  • 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.  
  • 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.  
  • 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.  
  • Scott IC, Blitz IL, Pappano WN; et al. (2001). "Homologues of Twisted gastrulation are extracellular cofactors in antagonism of BMP signalling". Nature 410 (6827): 475–8.  
  • 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.  
  • 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.  
  • 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.  
  • 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.  
  • Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903.  
  • 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.  
  • 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.  
  • 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.  
  • Hillman RT, Green RE, Brenner SE (2005). "An unappreciated role for RNA surveillance". Genome Biol. 5 (2): R8.  

External links

  • The MEROPS online database for peptidases and their inhibitors: M12.005

External links


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