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The 1.8 Å crystal structure of ACTIBIND suggests a mode of action for T2 ribonucleases as antitumorigenic agents.

Abstract：

: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 Å 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.

journal_name

J Med Chem

journal_title

Journal of medicinal chemistry

authors

de Leeuw M,González A,Lanir A,Roiz L,Smirnoff P,Schwartz B,Shoseyov O,Almog O

doi

10.1021/jm1015507

subject

Has Abstract

pub_date

2012-02-09 00:00:00

pages

1013-20

issue

3

eissn

0022-2623

issn

1520-4804

journal_volume

55

pub_type

杂志文章

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