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A zinc ion sits at the bottom of the cleft and is coordinated in a trigonal-bipyramidal geometry by three histidine residues, a tyrosine residue Tyrand 2637 water molecule, which is also bound to the carboxylic acid side chain of Glu Search for related content.

Lane 114 C-labeled type I procollagen 0.

This raised the possibility that Cys 85 could form a disulfide bond with a cysteine other than Cys In brief, a peptide corresponding to the 10 N-terminal residues of the mature BMP-1 protein after removal of the prodomain was conjugated to keyhole limpet hemocyanin 2637 subsequently used to immunize two separate rabbits. This indicated that the Cys 63 and Cys 65 mutant molecules have a more open conformation than the wild-type molecule.

The results showed that BMP-1myc was secreted into the culture medium mostly as the mature enzyme. The sequence alignment of astacin and BMP This xs a direct analogy with what happens in astacin when Trp 65 the equivalent of Cys 66 in BMP-1 backs onto the P1 position of the astacin substrate. Responses Submit a Letter to the Editor. Green indicates identical residues. In the absence of structural information of the metalloproteinase domain of BMP-1 we reasoned that a valid approach was to examine the function of individual residues by 26273 mutagenesis.

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BMP-1myc was examined by Western blot analysis in which the primary antibody was either the mouse monoclonal anti-c-myc peptide antibody, 9E10, or the rabbit neoepitope polyclonal antibody. This included astacin, BMP-1, mammalian tolloid, mammalian tolloid-like-1, mammalian tolloid-like-2, and meprins.


Cells in RIPA buffer were scraped on ice and sonicated. Lane 214 C-labeled procollagen 0. In astacin, the equivalent cysteine Cys 64 forms a vital disulfide bond with a non-active site cysteine Cys Cleavage of type I procollagen by recombinant BMP-1myc analyzed under non-reducing conditions.

Assay of Procollagen C-proteinase Recombinant BMP-1 was assayed for procollagen C-proteinase activity using human 14 C-labeled type I d substrate and analysis of the cleavage products on SDS gels as described 3.

Cell lysates contained only the latent form of BMP Furthermore, the culture medium from COS-7 cells transfected with the empty vector contained no immunoreactive proteins, which shows that the endogenous levels of BMP-1 were very low. The importance of Cys 85 in stabilizing the structure of the metalloproteinase domain of BMP-1 was confirmed when C85A was found to be poorly secreted.

The numbers of the metalloproteinase domain can be converted to the cs in the BMP-1 sequence by adding The metalloproteinase domain of astacin is kidney-shaped and has two domains at the N and C termini that are separated by an active site cleft Cleavage occurs between a specific alanine or glycine residue depending on the procollagen chain and an invariant aspartic acid residue in each of the three chains of procollagen.

Rs preliminary studies we performed a multiple sequence alignment of 31 members of the astacin family of metalloproteinases using MultAlin 25 data not shown.

In some experiments we noticed that latent BMP-1 was detected in the culture medium. This approach is made possible by the fact that the metalloproteinase domain of BMP-1 shares high sequence homology with astacin, whose x-ray crystal structure is known Although the metalloproteinase domains of astacin and BMP-1 are homologous and presumably have a similar tertiary structure, it is not obvious why BMP-1 2237 scissile bonds between a small side chained residue and an aspartic acid.


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Non-immune serum was collected prior to injections. It has been suggested that the equivalent disulfide bond in BMP-1 is formed between Cys 65 and Cys 85 These results indicated that Lys 87 and Lys act together to stabilize enzyme-substrate interactions involving the primed side of the substrate.

Pwo DNA polymerase was used to minimize base misincorporation during the polymerase chain reactions. The polyclonal antibody was raised, by Sigma, in rabbits using conventional procedures.

The Xcm I site is located at nucleotide The occurrence of abnormal fibrils in affected tissues of this mouse is consistent with the persistence of partially processed procollagen molecules.

Western blot analysis showed that sd antibody recognized the C-propeptides after cleavage of procollagen with recombinant BMP-1 and BMP-1myc data not shown.

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The Dss I site is located at nucleotide The absence of the Cys 63 -Cys 66 disulfide bond in 1 the Cys 66 mutant, 2 the Cys 63 mutant because Cys 66 has a free thiol group in this mutantand 3 the Cys 65 mutant because Cys 85 has bonded with Cys 63 thus leaving a free thiol group on Cys 66 alters the chemical structure of the S1 site and decreases PCP activity. Further experiments showed that Cys 66 and Cys 63which are located in the tolloid-specific sequence Cys 63 -Gly 64 -Cys 65 -Cys 66 in the active site, most likely form es disulfide bridge.

Surprisingly, however, the Cys 65 mutant was secreted efficiently.