STRUCTURE OF ACTABIND

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This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. ACTIBIND is a RNA catalyzing enzyme (ribonuclase or RNase) which is produced by Aspergillus niger. RNases are ubiquitous and efficient enzymes which hydrolyze RNA to 3' mononucleotides via 2', 3' cyclic nucleotides. Due to its ability to bind actin and to interfere with the cytoskeletal network structure, ACTIBIND has antitumorigenic and antiangiogenic properties in mice, unrelated to its Rnase activity. The structure of ACTIBIND has been solved by molecular replacement and refined to 1.7 A resolution. The refined model has two N-glycosylation sites, both of which are also found in other related R-Nases. The active site shows a strongly bound phosphate and planar disociated density which may correspond to the ribose-base moiety of RNA.