3tbj | pdb_00003tbj

The 1.7A crystal structure of Actibind a T2 ribonucleases as antitumorigenic agents

spinqualitylabelsall models 3tbj, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3tbj is a 1 chain structure with sequence from Aspergillus niger. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: EDO, NAG, PO4 Related: 3d3z Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed ACTIBIND and its human homologue RNASET2 are T2 ribonucleases (RNases). RNases are ubiquitous and efficient enzymes that hydrolyze RNA to 3' mononucleotides and also possess antitumorigenic and antiangiogenic activities. Previously, we have shown that ACTIBIND and RNASET2 bind actin and interfere with the cytoskeletal network structure, thereby inhibiting cell motility and invasiveness in cancer and in endothelial cells. We also showed that ACTIBIND binds actin in a molar ratio of 1:2. Here, we further characterize ACTIBIND and determine its crystal structure at 1.8 A resolution, which enables us to propose two structural elements that create binding sites to actin. We suggest that each of these binding sites is composed of one cysteine residue and one conserved amino acid region. These binding sites possibly interfere with the cytoskeleton network structure and as such may be responsible for the antitumorigenic and antiangiogenic activities of ACTIBIND and its human analogue RNASET2. The 1.8 A crystal structure of ACTIBIND suggests a mode of action for T2 ribonucleases as antitumorigenic agents.,de Leeuw M, Gonzalez A, Lanir A, Roiz L, Smirnoff P, Schwartz B, Shoseyov O, Almog O J Med Chem. 2012 Feb 9;55(3):1013-20. Epub 2012 Jan 31. PMID:22216760 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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