Department of Clinical and Experimental Medicine - Endocrinology, University of Messina, via Consolare Valeria - Gazzi, 98125 Messina, Italy.
Department of Clinical and Experimental Medicine - Dermatology, University of Messina, via Consolare Valeria - Gazzi, 98125 Messina, Italy,
Front Biosci (Landmark Ed). 2019 Jan 1;24(2):212-230. doi: 10.2741/4714.
A phylogenetically conserved 5-residue thyroid hormone (TH)- binding motif was originally found in a few TH plasma carriers and, more recently, in all known plasma and cell-associated proteins interacting with TH as well as in proteins involved in iodide uptake. Minor variations of the motif were found, depending on the particular class of those proteins. Since thyroglobulin (Tg) is the protein matrix for TH synthesis starting from iodination of a selected number of tyrosines (to form first monoiodotyrosine (MIT) and diiodotyrosine (DIT) and then T3 and T4), we hypothesized that by searching the presence of perfect or imperfect versions of that motif in two Tg species (human and murine) in which the iodinated tyrosines and pattern of iodotyrosine/iodothyronine formation are known, we could have found relevant explanations. Explanations, which are not furnished by the simple possession of tyrosine-iodination motifs and sequence of the iodination motif, concern why only some (but not other) tyrosine residues in one species are iodinated and why they have a particular iodination pattern. In this bioinformatics study, we provide such explanations.
一个在进化上保守的 5 个氨基酸残基的甲状腺激素 (TH) 结合基序最初在少数几个 TH 血浆载体中被发现，最近在所有已知与 TH 相互作用的血浆和细胞相关蛋白以及参与碘摄取的蛋白中被发现。由于甲状腺球蛋白 (Tg) 是从甲状腺激素合成的起始蛋白基质，碘化了一些酪氨酸（形成第一个单碘酪氨酸 (MIT) 和二碘酪氨酸 (DIT)，然后是 T3 和 T4），因此我们假设通过在两种 Tg 物种（人和鼠）中搜索该基序的完整或不完整版本，已知其碘化酪氨酸和碘酪氨酸/甲状腺素形成的模式，我们可以找到相关的解释。这些解释不能仅仅通过酪氨酸碘化基序和碘化基序的序列来提供，涉及为什么在一个物种中只有一些（而不是其他）酪氨酸残基被碘化，以及为什么它们具有特定的碘化模式。在这项生物信息学研究中，我们提供了这样的解释。
