完整的氨基酸序列的连锁人血浆hs-glycoproteinα2。
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吉冈Y, Gejyo F,马蒂T, Rickli EE, Burgi W, Offner GD,特射频,施密德K
完整的氨基酸序列的连锁人血浆hs-glycoproteinα2。
J生物化学杂志。1986年2月5日,261 (4):1665 - 76。
- PubMed ID
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3944104 (在PubMed]
- 文摘
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正常人血浆α2 hs-glycoprotein早些时候已被证明是由两个多肽链。最近,短链的氨基酸和碳水化合物序列是阐明(Gejyo F。、常J.-L。Burgi, W。施密德,K。、Offner g D。特,水范Halbeck, H。Dorland, L。要,g . J。,Vliegenthart J.F.G.(1983)生物。258年化学,4966 - 4971)。在目前的研究中,长链的氨基酸序列的蛋白质,指定连锁,决心,发现由282个氨基酸残基组成。24个氨基酸的句子被发现; the most abundant of these are Pro-Pro and Ala-Ala which each occur five times. Of particular interest is the presence of three Gly-X-Pro and one Gly-Pro-X sequences that are characteristic of the repeating sequences of collagens. Chou-Fasman evaluation of the secondary structure suggested that the A-chain contains 29% alpha-helix, 24% beta-pleated sheet, and 26% reverse turns and, thus, approximately 80% of the polypeptide chain may display ordered structure. Four glycosylation sites were identified. The two N-glycosidic oligosaccharides were found in the center region (residues 138 and 158), whereas the two O-glycosidic heterosaccharides, both linked to threonine (residues 238 and 252), occur within the carboxyl-terminal region. The N-glycans are linked to Asn residues in beta-turns, while the O-glycans are located in short random segments. Comparison of the sequence of the amino- and carboxyl-terminal 30 residues with protein sequences in a data bank demonstrated that the A-chain is not significantly related to any known proteins. However, the proline-rich carboxyl-terminal region of the A-chain displays some sequence similarity to collagens and the collagen-like domains of complement subcomponent C1q.