Mouse relaxin: synthesis and biological activity of the first relaxin with an unusual crosslinking pattern.
Mouse relaxin: synthesis and biological activity of the first relaxin with an unusual crosslinking pattern.
复制标题
小鼠松弛素：第一个具有不寻常交联模式的松弛素的合成和生物活性。
DOI：
10.1006/bbrc.1993.2250
复制
发表时间：
1993
影响因子：
3.1
通讯作者：
Schwabe,C
中科院分区：
文献类型：
--
作者：
Bullesbach,EE;Schwabe,C
根据最近公布的cDNA序列，小鼠松弛素在A链的C末端具有额外的氨基酸，因此由25个氨基酸组成的链间环而不是通常的24元环。由于限制性二硫键排列，预期额外残基可导致C-末端α-螺旋中的环出。我们已经化学合成了真正的小鼠松弛素以及类似物没有额外的A链残基，并发现，天然激素，虽然活跃，是劣于其胰岛素样类似物。这一结果与我们先前的研究一致，该研究表明松弛素的表面由A链的C-末端螺旋表示，位于包含受体相互作用位点的表面的对面，因此对修饰不太敏感。
According to a recently published cDNA sequence, mouse relaxin has an extra amino acid in the C-terminal end of the A chain and thus an interchain loop consisting of 25 amino acids instead of the usual 24-membered ring. Because of the restrictive disulfide link arrangement the extraresidue can be expected to cause a loop out in the C-terminal α-helix. We have chemically synthesized authentic mouse relaxin as well as an analog without the additional A chain residue and found that the native hormone, although active, was inferior to its insulin-like analog. This result is in harmony with our previous study which suggests that the surface of relaxin represented by the C-terminal helix of the A chain is positioned opposite to the surface that contains the receptor interaction site and therefore is less sensitive to modifications.