2004
DOI: 10.1016/j.bbrc.2004.06.072
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Structure and expression of an unusually acidic matrix protein of pearl oyster shells

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Cited by 192 publications
(182 citation statements)
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“…In addition, the amino acid composition of Prisilkin-39 is also comparable with that of crude matrix proteins from the prismatic layer of P. fucata (41). In contrast to many other shell matrix proteins singularly enriched in Asp and Glu residues (12)(13)(14)(15)(16), the occurrence of these acidic amino acids in Prisilkin-39 is markedly low, with only one Asp residue. Thus, Prisilkin-39 belongs to the rare group of basic matrix proteins with a theoretical pI of 8.83.…”
Section: Characterization Of Deduced Amino Acid Sequence Ofmentioning
confidence: 70%
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“…In addition, the amino acid composition of Prisilkin-39 is also comparable with that of crude matrix proteins from the prismatic layer of P. fucata (41). In contrast to many other shell matrix proteins singularly enriched in Asp and Glu residues (12)(13)(14)(15)(16), the occurrence of these acidic amino acids in Prisilkin-39 is markedly low, with only one Asp residue. Thus, Prisilkin-39 belongs to the rare group of basic matrix proteins with a theoretical pI of 8.83.…”
Section: Characterization Of Deduced Amino Acid Sequence Ofmentioning
confidence: 70%
“…Based on a comparative analysis of currently known molluscan shell proteins according to the different shell layers in which they are present, the interesting phenomenon of an unbalanced protein distribution pattern has been discovered. It mainly embodies the fact that all of the extremely acidic shell proteins (pI Ͻ 4.5) are preferentially associated with the calcitic prismatic layer rather than the aragonitic nacreous layer (4,5,(12)(13)(14)(15)(16). Acidic matrix proteins are believed to be the major components in the soluble fraction of the shell matrix, and they exert effective control over the crystal growth because of their cation-binding capacity (17)(18)(19)(20).…”
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confidence: 99%
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“…A probable relationship between the chemical features of biomolecules and crystal growth control is supported by many observations showing that proteins isolated from sites of biomineralization in tissues are unusually enriched in highly acidic amino acids, notably aspartic acid and also glutamic acid (9)(10)(11)(12)(13). The Asp-rich motifs have been postulated to function by preferentially binding to cations such as Ca 2ϩ (14) during the controlled formation of minerals such as calcite (12).…”
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confidence: 96%