The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism.
The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism.
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牛蛋白酪氨酸磷酸酶二聚体的结构揭示了潜在的自我调节机制。
DOI：
10.1021/bi990381x
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发表时间：
1999
期刊：
影响因子：
2.9
通讯作者：
Stauffacher,CV
中科院分区：
文献类型：
--
作者：
Tabernero,L;Evans,BN;Tishmack,PA;VanEtten,RL;Stauffacher,CV
The bovine protein tyrosine phosphatase (BPTP) is a member of the class of low-molecular weight protein tyrosine phosphatases (PTPases) found to be ubiquitous in mammalian cells. The catalytic site of BPTP contains a CX5R(S/T) phosphate-binding motif or P-loop (residues 12−19) which is the signature sequence for all PTPases. Ser19, the final residue of the P-loop motif, interacts with the catalytic Cys12 and participates in stabilizing the conformation of the active site through interactions with Asn15, also in the P-loop. Mutations at Ser19 result in an enzyme with altered kinetic properties with changes in the pKaof the neighboring His72. The X-ray structure of the S19A mutant enzyme shows that the general conformation of the P-loop is preserved. However, changes in the loop containing His72 result in a displacement of the His72 side chain that may explain the shift in the pKa. In addition, it was found that in the crystal, the protein forms a dimer in which Tyr131 and Tyr132 from one monomer insert into the active site of the other monomer, suggesting a dual-tyrosine motif on target sites for this enzyme. Since the activity of this PTPase is reportedly regulated by phosphorylation at Tyr131 and Tyr132, the structure of this dimer may provide a model of a self-regulation mechanism for the low-molecular weight PTPases.
人肝脏酸性磷酸酶。
DOI：
--
发表时间：
1975
期刊：
Hoppe-Seyler´s Zeitschrift für physiologische Chemie
影响因子：
--
作者：
D. M. Rehkop;R. L. Etten
通讯作者：
R. L. Etten