Lowe J B, Boguski M S, Sweetser D A, Elshourbagy N A, Taylor J M, Gordon J I
J Biol Chem. 1985 Mar 25;260(6):3413-7.
We have determined the primary structure of human liver fatty acid binding protein from an analysis of a full length cDNA. This 127-residue 14,178-Da protein exhibits a high degree of sequence conservation when compared to its orthologous homologue, rat liver fatty acid binding protein. It appears likely that this polypeptide arose from two intragenic duplication events. Using a variety of computational techniques, we were unable to find any evidence of amphipathic alpha helical domains in this protein nor any sequence similarities to apolipoproteins and serum albumins. A family of paralogous proteins was defined, whose members share a remarkable degree of sequence homology with share a remarkable degree of sequence homology with human liver fatty acid binding protein. These include rat intestinal fatty acid binding protein, the cellular the P2 protein of myelin. It appears that the small cytosolic fatty acid binding proteins have evolved structural features necessary for lipid-protein interaction which are different from those present in some familiar and better studied extracellular sequences.
通过对全长cDNA的分析，我们确定了人肝脏脂肪酸结合蛋白的一级结构。这种由127个氨基酸残基组成、分子量为14178道尔顿的蛋白质，与它的直系同源物大鼠肝脏脂肪酸结合蛋白相比，表现出高度的序列保守性。这种多肽似乎是由两次基因内重复事件产生的。使用各种计算技术，我们在该蛋白质中未能找到任何两亲性α螺旋结构域的证据，也未发现与载脂蛋白和血清白蛋白的任何序列相似性。定义了一个旁系同源蛋白家族，其成员与人类肝脏脂肪酸结合蛋白具有显著程度的序列同源性。这些包括大鼠肠道脂肪酸结合蛋白、髓磷脂的细胞P2蛋白。看来，小的胞质脂肪酸结合蛋白已经进化出了脂质-蛋白质相互作用所需的结构特征，这些特征与一些为人熟知且研究较多的细胞外序列中的特征不同。
