Crystal structure of human V-1 in the apo form

V-1, also known as myotrophin, is a 13   kDa ankyrin-repeat protein that binds and inhibits the heterodimeric actin capping protein (CP), which is a key regulator of cytoskeletal actin dynamics. The crystal structure of V-1 in complex with CP revealed that V-1 recognizes CP via residues spanning several ankyrin repeats. Here, the crystal structure of human V-1 is reported in the absence of the specific ligand at 2.3   Å resolution. In the asymmetric unit, the crystal contains two V-1 monomers that exhibit nearly identical structures (C α r.m.s.d. of 0.47   Å ). The overall structures of the two apo V-1 chains are also highly similar to that of CP-bound V-1 (C α r.m.s.d.s of

Source: Acta Crystallographica Section F - January 1, 2021 Category: Biochemistry Authors: Takeda, S. Koike, R. Nagae, T. Fujiwara, I. Narita, A. Ma é da, Y. Ota, M. Tags: V-1 myotrophin actin capping protein crystal structure All Atom Motion Tree ankyrin-repeat proteins research communications Source Type: research