2VEV

CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B IN COMPLEX WITH AN ISOTHIAZOLIDINONE-CONTAINING INHIBITOR

Summary for 2VEV

• Entry DOI: 10.2210/pdb2vev/pdb
• Related: 1A5Y 1AAX 1BZC 1BZH 1BZJ 1C83 1C84 1C85 1C86 1C87 1C88 1ECV 1EEN 1EEO 1G1F 1G1G 1G1H 1G7F 1G7G 1GFY 1I57 1JF7 1KAK 1KAV 1L8G 1LQF 1NL9 1NNY 1NO6 1NWE 1NWL 1NZ7 1OEM 1OEO 1OES 1OET 1OEU 1OEV 1ONY 1ONZ 1PA1 1PH0 1PTT 1PTU 1PTV 1PTY 1PXH 1PYN 1Q1M 1Q6J 1Q6M 1Q6N 1Q6P 1Q6S 1Q6T 1QXK 1SUG 1T48 1T49 1T4J 1WAX 1XBO 2AZR 2B07 2B4S 2BGD 2BGE 2CM2 2CM3 2CM7 2CM8 2CMA 2CMB 2CMC 2CNE 2CNF 2CNG 2CNH 2CNI 2F6F 2F6T 2F6V 2F6W 2F6Y 2F6Z 2F70 2F71 2FJM 2FJN 2HNP 2HNQ 2VEU 2VEW 2VEX 2VEY
• Descriptor: TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1, N-[(1S)-1-(4-benzyl-1H-imidazol-2-yl)-2-{4-[(5S)-1,1-dioxido-3-oxoisothiazolidin-5-yl]phenyl}ethyl]-3-(trifluoromethyl)benzenesulfonamide, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: membrane, oxidation, hydrolase, acetylation, phosphatase, polymorphism, phosphorylation, protein phosphatase, endoplasmic reticulum
• Biological source: HOMO SAPIENS (HUMAN)
• Total number of polymer chains: 1
• Total formula weight: 38008.59

Authors

Douty, B.,Wayland, B.,Ala, P.J.,Bower, M.J.,Pruitt, J.,Bostrom, L.,Wei, M.,Klabe, R.,Gonneville, L.,Wynn, R.,Burn, T.C.,Liu, P.C.C.,Combs, A.P.,Yue, E.W. (deposition date: 2007-10-27, release date: 2007-11-06, Last modification date: 2024-05-08)

Primary citation

Douty, B.,Wayland, B.,Ala, P.J.,Bower, M.J.,Pruitt, J.,Bostrom, L.,Wei, M.,Klabe, R.,Gonneville, L.,Wynn, R.,Burn, T.C.,Liu, P.C.C.,Combs, A.P.,Yue, E.W.
Isothiazolidinone Inhibitors of Ptp1B Containing Imidazoles and Imidazolines
Bioorg.Med.Chem.Lett., 18:66-, 2008

PubMed Abstract: The structure-based design and synthesis of isothiazolidinone (IZD) inhibitors of PTP1B containing imidazoles and imidazolines and their modification to interact with the B site of PTP1B are described here. The X-ray crystal structures of 3I and 4I complexed with PTP1B were solved and revealed the inhibitors are interacting extensively with the B site of the enzyme.

PubMed: 18037290
DOI: 10.1016/J.BMCL.2007.11.012

Experimental method

X-RAY DIFFRACTION (1.8 Å)