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Publication : Molecular cloning of avian matrix Gla protein.

First Author  Wiedemann M Year  1998
Journal  Biochim Biophys Acta Volume  1395
Issue  1 Pages  47-9
PubMed ID  9434150 Mgi Jnum  J:44881
Mgi Id  MGI:1101427 Doi  10.1016/s0167-4781(97)00155-3
Citation  Wiedemann M, et al. (1998) Molecular cloning of avian matrix Gla protein. Biochim Biophys Acta 1395(1):47-9
abstractText  Matrix Gla protein plays an essential role in preventing the calcification of blood vessel walls, cartilage and other tissues. We report here the primary structure of chicken matrix Gla protein as deduced from the cDNA sequence. The avian protein exhibited the characteristic motifs previously identified in the mammalian proteins, but its amino acid sequence shared only 51-56% identity with the latter proteins. Moreover, a region proposed to function as binding site for gamma-carboxylase in the mammalian proteins was poorly conserved in the chicken protein. Our sequence data should be helpful in the design of mutational analyses which are intended to characterize functional interactions of matrix Gla proteins with other proteins.
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