DOI 10.5012/bkcs.2010.31.5.1397 Refined Structure of Human NM23-H1 from a Hexagonal Crystal

H1. Their approximate dimensions are 0.1 × 0.1 × 1.0 mm and the best crystal diffracted to 4.0 Å with high diffraction anisotropy. (B) Form 2 crystals of human NM23-H1. Their approximate dimensions are 0.3 × 0.3 × 0.3 mm and the best crystal diffracted to 2.1 Å. NM23-H1, also known as NDP kinase A (NDK-A), is the first identified metastasis suppressor gene.1 It catalyzes the transfer of γ-phosphoryl group from a nucleoside triphosphate (NTP) donor onto a nucleoside diphosphate (NDP) acceptor through a transiently phosphorylated histidine residue. Other enzymatic activities of NM23-H1 include histidine kinase and 3’-5 ’ exo-nuclease activity.2 NM23-H1 shows high sequence identity to hexameric NM23-H2 (NDK-B), another member of NDK fa-mily.3 Multiple proteins including CKI, Aurora-A, Tiam1, Dbl1, KSR, ST-RAP and h-Prune have been reported to bind NM23