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Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella11:31

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Ionic crystals consist of two or more different kinds of ions that usually have different sizes. The packing of these ions into a crystal structure is more complex than the packing of metal atoms that are the same size.
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Related Experiment Video

Updated: Jan 20, 2026

Crystal Structure of the N-terminal Domain of Ryanodine Receptor from Plutella xylostella
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Crystal structure of human YTHDC2 YTH domain.

Chao Ma1, Shanhui Liao1, Zhongliang Zhu1

  • 1Hefei National Laboratory for Physical Sciences at the Microscale and School of Life Sciences, University of Science and Technology of China, 230027, Hefei, China.

Biochemical and Biophysical Research Communications
|September 2, 2019
PubMed
Summary
This summary is machine-generated.

YTHDC2, an N6-methyladenosine (m6A) reader, is crucial for fertility. This study reveals the crystal structure of its YTH domain, uncovering its m6A RNA binding mechanism.

Keywords:
Crystal structureYTH domainYTHDC2m(6)A RNA

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Area of Science:

  • Molecular Biology
  • Structural Biology
  • Epigenetics

Background:

  • N6-methyladenosine (m6A) is a key epigenetic modification regulating mRNA functions.
  • m6A
  • readers
  • interpret the m6A mark, influencing mRNA metabolism and function.
  • YTHDC2 is an m6A reader protein implicated in fertility regulation.

Purpose of the Study:

  • To elucidate the molecular mechanism by which the YTH domain of YTHDC2 recognizes m6A-modified RNA.
  • To determine the crystal structure of the human YTHDC2 YTH domain.

Main Methods:

  • X-ray crystallography was employed to determine the 3D structure of the YTHDC2 YTH domain.
  • Structural analysis was performed to identify conserved m6A binding pockets and RNA interaction surfaces.

Main Results:

  • The crystal structure of the human YTHDC2 YTH domain was determined, revealing an architecture conserved among YTH domain proteins.
  • A conserved m6A binding pocket within the YTHDC2 YTH domain was identified.
  • The YTHDC2 YTH domain shares a similar RNA binding surface with YTHDC1.

Conclusions:

  • The determined structure provides insights into the m6A RNA recognition mechanism of YTHDC2.
  • Understanding YTHDC2's m6A binding is crucial for comprehending its role in fertility and mRNA regulation.
  • Structural similarities suggest conserved functions among YTH domain readers.