Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.1.3.48 extracted from

  • Fang, L.; Zhang, H.; Cui, W.; Ji, M.
    Studies of the mechanism of selectivity of protein tyrosine phosphatase 1B (PTP1B) bidentate inhibitors using molecular dynamics simulations and free energy calculations (2008), J. Chem. Inf. Model., 48, 2030-2041.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information mechanism of substrate selectivity of five bidentate inhibitors, NNY, B07, F6Z, Q1M, and PYN, for PTP1B, compared to SHP-2 and TCPTP, using molecular dynamics simulations and free energy calculations, and crystal structures with PDB IDs 1NNY, 2B07, 2F6Z, 1Q1M, and 1PYN, 1L8k, and 2SHP, overview. Residues Arg24, Arg254, and Gln262 in the second binding site of PTP1B are essential for the high selectivity of inhibitors Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Synonyms

Synonyms Comment Organism
protein tyrosine phosphatase 1B
-
Homo sapiens
PTP1B
-
Homo sapiens
SHP-2
-
Homo sapiens
TCPTP
-
Homo sapiens

General Information

General Information Comment Organism
malfunction PTPB1 is involved in type II diabetes Homo sapiens