PEPTIDE REPEATS IN A MUSSEL GLUE PROTEIN - THEME AND VARIATIONS
PEPTIDE REPEATS IN A MUSSEL GLUE PROTEIN - THEME AND VARIATIONS
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DOI:
10.1021/bi00340a008
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发表时间:
1985-01-01
期刊:
影响因子:
2.9
通讯作者:
TANZER, ML
中科院分区:
文献类型:
--
作者:
WAITE, JH;HOUSLEY, TJ;TANZER, ML
The adhesive protein from Mytilus edulis contains 75-80 closely related, repeated peptide sequences in its primary structure. These peptides can be resolved following digestion with trypsin by reversed-phase high-pressure liquid chromatography. The most frequency repeated sequence is the decapeptide Ala-Lys-Pro-Ser-Tyr-Hyp-Hyp-Thr-Dopa-Lys (peptide E). Variations of this occur in peptides B with Hyp-3 and Dopa-5, C with Dopa-5, and D with Hyp-3, respectively. Lesser amounts of hexapeptides (A and B'') that are lacking residues 4-7 also occur. Peptide A has the sequence Ala-Lys-Pro-Thr-Dopa-Lys, whereas B'' contains Tyr instead of Dopa. 4-Hydroxyproline occurs at positions 3 and 7 and occasionally at position 6 of the decapeptide; 3-hydroxyproline occurs only at position 6. Adhesiveness of the protein may be related to the repetition of Dopa residues, the catecholic moiety of which has strong hydrogen-bonding and metal-liganding capabilities.