Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response.

Abstract

Human arginase I is a potential target for therapeutic intervention in diseases linked to compromised l-arginine homeostasis. Here, we report high-affinity binding of the reaction coordinate analogue inhibitors 2(S)-amino-6-boronohexanoic acid (ABH, Kd = 5 nM) and S-(2-boronoethyl)-l-cysteine (BEC, Kd = 270 nM) to human arginase I, and we report x-ray… (More)

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@article{Costanzo2005CrystalSO, title={Crystal structure of human arginase I at 1.29-A resolution and exploration of inhibition in the immune response.}, author={Luigi Di Costanzo and Guadalupe Sabio and Alfonso Mora and Paulo C. Rodriguez and Augusto Ochoa and Francisco Centeno and David W Christianson}, journal={Proceedings of the National Academy of Sciences of the United States of America}, year={2005}, volume={102 37}, pages={13058-63} }