7DF7

Crystal structure of human V-1 in the apo form

Summary for 7DF7

• Entry DOI: 10.2210/pdb7df7/pdb
• Descriptor: Myotrophin (2 entities in total)
• Functional Keywords: actin dynamics, ankyrin repeat protein, actin capping protein, cytosolic protein
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 2
• Total formula weight: 26648.48

Authors

Takeda, S.,Nagae, T. (deposition date: 2020-11-06, release date: 2021-01-20, Last modification date: 2024-11-20)

Primary citation

Takeda, S.,Koike, R.,Nagae, T.,Fujiwara, I.,Narita, A.,Maeda, Y.,Ota, M.
Crystal structure of human V-1 in the apo form.
Acta Crystallogr.,Sect.F, 77:13-21, 2021

PubMed Abstract: 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 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 r.m.s.d.s of <0.50 Å), indicating that CP does not induce a large conformational change in V-1. Detailed structural comparisons using the computational program All Atom Motion Tree revealed that CP binding can be accomplished by minor side-chain rearrangements of several residues. These findings are consistent with the known biological role of V-1, in which it globally inhibits CP in the cytoplasm.

PubMed: 33439151
DOI: 10.1107/S2053230X20016829

Experimental method

X-RAY DIFFRACTION (2.3 Å)