HUMAN-PLACENTA PROTEIN-TYROSINE-PHOSPHATASE - AMINO-ACID SEQUENCE AND RELATIONSHIP TO A FAMILY OF RECEPTOR-LIKE PROTEINS
HUMAN-PLACENTA PROTEIN-TYROSINE-PHOSPHATASE - AMINO-ACID SEQUENCE AND RELATIONSHIP TO A FAMILY OF RECEPTOR-LIKE PROTEINS
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DOI：
10.1073/pnas.86.14.5252
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发表时间：
1989-07-01
影响因子：
11.1
通讯作者：
WALSH, KA
中科院分区：
文献类型：
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作者：
CHARBONNEAU, H;TONKS, NK;WALSH, KA
已经确定了胞质人类胎盘蛋白酪氨酸磷酸酶1B（PTP 1B;蛋白酪氨酸磷酸磷酸水解酶，EC 3.1.3.48）的氨基酸序列。它由321个残基的单链组成，具有N-乙酰化的N-末端甲硫氨酸和异常富含脯氨酸的C-末端区域。该酶在结构上与白细胞共同抗原CD 45和LAR的两个胞质结构域相关，LAR是一种具有类似于神经细胞粘附分子的外部片段的CD 45样分子。由来自T细胞的cDNA克隆编码的低分子量蛋白质也显示出广泛的序列相似性。本研究定义了这个不同的PTPases家族共同的同源结构域，包括可溶性和受体样跨膜形式。半胱氨酸残基121和215的PTD 1B是保守的家庭中的所有成员，并参与催化的候选人，因为PTD 1B是由硫醇修饰剂失活。富含带正电荷残基的两个区段（残基33-47和227-238）可提供与抑制性阴离子聚合物（如肝素或聚（Glu/Tyr））相互作用的位点。
The amino acid sequence of the cytosolic human placenta protein-tyrosine-phosphatase 1B (PTPase 1B; protein-tyrosine-phosphate phosphohydrolase, EC 3.1.3.48) has been determined. It consists of a single chain of 321 residues with an N-acetylated N-terminal methionine and an unusually proline-rich C-terminal region. The enzyme is structurally related to the two cytoplasmic domains of both the leukocyte common antigen CD45 and LAR, a CD45-like molecule with an external segment that resembles a neural cell adhesion molecule. A low molecular weight protein encoded by a cDNA clone from T cells also shows extensive sequence similarities. The present study defines homologous domains common to this diverse family of PTPases that includes both soluble and receptor-like transmembrane forms. The cyseinyl residues 121 and 215 of PTPase 1B are conserved among all members of the family and are candidates for involvement in catalysis since PTPase 1B is inactivated by thiol modifying reagents. Two segments rich in positively charged residues (residues 33-47 and 227-238) may provide sites of interaction with inhibitory anionic polymers such as heparin or poly(Glu/Tyr).