COMPARATIVE STRUCTURAL-ANALYSIS OF DESMOPLAKIN, BULLOUS PEMPHIGOID ANTIGEN AND PLECTIN - MEMBERS OF A NEW GENE FAMILY INVOLVED IN ORGANIZATION OF INTERMEDIATE FILAMENTS
COMPARATIVE STRUCTURAL-ANALYSIS OF DESMOPLAKIN, BULLOUS PEMPHIGOID ANTIGEN AND PLECTIN - MEMBERS OF A NEW GENE FAMILY INVOLVED IN ORGANIZATION OF INTERMEDIATE FILAMENTS
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DOI：
10.1016/s0141-8130(05)80004-2
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发表时间：
1992-06-01
影响因子：
8.2
通讯作者：
PARRY, DAD
中科院分区：
文献类型：
--
作者：
GREEN, KJ;VIRATA, MLA;PARRY, DAD
桥粒斑蛋白（DP）和大疱性类天疱疮抗原（BPA）分别是桥粒和半桥粒的主要斑块成分。这些细胞粘附结构都与中间丝（IF）网络密切相关。DP和BPA序列的结构分析表明，这些分子很可能形成延伸的哑铃形二聚体与中心杆和球状端域。最近的序列数据表明DP和BPA的N-末端结构域（如它们的C-末端结构域）是高度相关的&前者含有七肽重复序列的区域，预测这些重复序列形成几个α-螺旋束。DP和BPA蛋白质序列与466 kDa的IF相关蛋白质的plectin（PL）序列的比较也揭示了大规模的同源性。它们的N端结构域之间的同一性为：DP：BPA = 35%，DP：PL = 32%，BPA：PL = 40%，表明BPA在该区域与PL的关系比DP更密切。然而，在含有38个残基重复基序的C-末端结构域中，DP和PL是更近的亲戚（同一性：DP：BPA = 38%，BPA：PL = 40%，DP：PL = 49%）。所有三种蛋白质的中心结构域具有广泛的七肽重复子结构，表达相同的周期性分布的带电残基，并预测形成双链α-螺旋卷曲螺旋绳。这些观察结果表明，DP，BPA和PL属于一个新的基因家族编码的蛋白质参与IF组织。
Desmoplakins (DP) and bullous pemphigoid antigen (BPA) are major plaque components of the desmosome and hemidesmosome, respectively. These cell adhesion structures are both associated intimately with the intermediate filament (IF) network. Structural analyses of DP and BPA sequences have indicated that these molecules are likely to form extended dumbbell-shaped dimers with a central rod and globular end domains. Recent sequence data have indicated that the N-terminal domains of both DP and BPA (like their C-terminal domains) are highly relate& the former contain regions of heptad repeats that are predicted to form several alpha-helical bundles. Comparisons of DP and BPA protein sequences with that of plectin (PL), a 466 kDa IF-associated protein, have also revealed large scale homology. Identities between their N-terminal domains are: DP:BPA = 35%, DP:PL = 32%, BPA:PL = 40%, suggesting that BPA is more closely related to PL than DP in this region. In the C-terminal domains, which contain a 38-residue repeating motif, however, DP and PL are closer relatives (identities: DP:BPA = 38%, BPA:PL = 40%, DP:PL = 49%). The central domains of all three proteins have extensive heptad repeat substructure, express the same periodic distribution of charged residues, and are predicted to form two-stranded alpha-helical coiled-coil ropes. These observations suggest that DP, BPA and PL belong to a new gene family encoding proteins involved in IF organization.