2KVK

Solution structure of ADF/cofilin (LDCOF) from Leishmania donovani

「2KD5」から置き換えられました

2KVK の概要

• エントリーDOI: 10.2210/pdb2kvk/pdb
• 分子名称: Actin severing and dynamics regulatory protein (1 entity in total)
• 機能のキーワード: adf/cofilin, leishmania donovani, hormone
• 由来する生物種: Leishmania donovani
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16253.54

構造登録者

Pathak, P.P.,Pulavarti, S.V.,Jain, A.,Sahasrabuddhe, A.A.,Gupta, C.M.,Arora, A. (登録日: 2010-03-16, 公開日: 2010-07-28, 最終更新日: 2024-05-01)

主引用文献

Pathak, P.P.,Pulavarti, S.V.S.R.,Jain, A.,Sahasrabuddhe, A.A.,Gupta, C.M.,Arora, A.
Solution structure and dynamics of ADF/cofilin from Leishmania donovani
J.Struct.Biol., 172:219-224, 2010

PubMed Abstract: Leishmania donovani ADF/cofilin (LdCof) is a novel member of ADF/cofilin family. LdCof depolymerizes, but does not co-sediment with, rabbit muscle actin filaments. Its F-actin depolymerizing activity is pH independent. Further, it possesses weak F-actin severing activity. In order to better understand its characteristic properties, we have determined the solution NMR structure of LdCof and have analyzed protein backbone dynamics from (15)N-relaxation measurements. The structure of LdCof possesses a conserved ADF/cofilin fold with a central mixed β-sheet consisting of six β-strands which is surrounded by five α-helices. LdCof structure has conserved G/F-actin binding site which includes the characteristic long kinked α-helix (α3). LdCof binds to rabbit muscle ADP-G-actin with 1:1 stoichiometry (K(d)∼0.2μM). The F-actin binding site is not well formed and analysis of (15)N-relaxation data shows that residues in the β4-β5 loop region and C-terminal are relatively flexible, which seems to be a determinant for the low F-actin severing activity of LdCof.

PubMed: 20627129
DOI: 10.1016/j.jsb.2010.07.001

実験手法

SOLUTION NMR