Jörnvall H, Mutt V, Persson M
Hoppe Seylers Z Physiol Chem. 1982 May;363(5):475-83. doi: 10.1515/bchm2.1982.363.1.475.
The amino acid sequences of gastrointestinal hormones were compared in fragments of variable spans. Similarities within each of three peptide groups are extensive, but non-unique alignments were also noticed in the glucagon group. Use of different spans demonstrated that structural similarities are unevenly distributed in the gastrin family. Correct phasing was detected even for proteins with few identities and multi-shifted alignments (alcohol dehydrogenases). Tests for alignments among different groups of peptides revealed similarities between bombesin and glucagon or secretin, as well as between caerulein and litorin. Recently determined extended structures suggested the presence of a few deletions/insertions close to the middle of the molecules (two such positions missing in the gastrin-releasing peptide in relation to glucagon). The alignments appear to structurally link large groups of peptide hormones and active peptides. Similarities concentrate in the C-terminal parts, and gaps in the middle. These facts are consistent with known correlations with bioactivities. They also suggest the possibility of evolutionary connections among different peptides as well as corresponding relationships among their receptors.
对胃肠道激素的氨基酸序列进行了不同跨度片段的比较。三个肽组中每组内部的相似性都很广泛，但在胰高血糖素组中也注意到了非唯一的比对。使用不同的跨度表明，结构相似性在胃泌素家族中分布不均。即使对于同一性较少且有多移位比对的蛋白质（醇脱氢酶），也检测到了正确的相位。对不同肽组之间的比对测试揭示了蛙皮素与胰高血糖素或促胰液素之间以及雨蛙肽与荔枝肽之间的相似性。最近确定的延伸结构表明，在分子中部附近存在一些缺失/插入（与胰高血糖素相比，胃泌素释放肽在两个这样的位置缺失）。这些比对似乎在结构上连接了大量的肽激素和活性肽。相似性集中在C末端部分，中间有缺口。这些事实与已知的生物活性相关性一致。它们还表明了不同肽之间进化联系的可能性以及它们受体之间的相应关系。
