Related Experiment Video
Updated: Mar 23, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
Published on: November 30, 2018
Crystal Structure of Human Myotubularin-Related Protein 1 Provides Insight into the Structural Basis of Substrate
Seoung Min Bong1, Kka-bi Son2, Seung-Won Yang1
1Research institute, National Cancer Center, Goyang, Gyeonggi 10408, Republic of Korea.
Abstract:
Myotubularin-related protein 1 (MTMR1) is a phosphatase that belongs to the tyrosine/dual-specificity phosphatase superfamily. MTMR1 has been shown to use phosphatidylinositol 3-monophosphate (PI(3)P) and/or phosphatidylinositol 3,5-bisphosphate (PI(3,5)P2) as substrates. Here, we determined the crystal structure of human MTMR1. The refined model consists of the Pleckstrin homology (PH)-GRAM and phosphatase (PTP) domains. The overall structure was highly similar to the previously reported MTMR2 structure. Interestingly, two phosphate molecules were coordinated by strictly conserved residues located in the C(X)5R motif of the active site. Additionally, our biochemical studies confirmed the substrate specificity of MTMR1 for PI(3)P and PI(3,5)P2 over other phosphatidylinositol phosphates. Our structural and enzymatic analyses provide insight into the catalytic mechanism and biochemical properties of MTMR1.
More Related Videos
Related Concept Videos
Overview of Myosin Structure and Function
ATP Synthase: Structure
Assembly of Cytoskeletal Filaments
Gene Families
Occasionally these regions can be adapted to take on new roles within the organism, becoming novel genes...
Protein and Protein Structure
A protein's shape is critical to its function. For example, an enzyme...
Protein Folding

