Crystal structure of mouse dual-specificity tyrosine phosphorylation-regulated kinase 1A (mDYRK1A)

• 발행기관: 한국구조생물학회
• 저자명: Boram Min Jeong Seok Cha Yun Heui Kim Hyun-Soo Cho Kuglae Kim
• 간행물 정보: 『Biodesign』Vol 13, No 1, Mar, 1~6쪽, 전체 6쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2025.03.31

국문 초록

DYRK1A, a proline-directed serine/threonine and tyrosine kinase located within the Down syndrome critical region (DSCR) on chromosome 21, plays critical roles in neuronal development and brain physiology. While structural studies on human DYRK1A have been extensively conducted, structural data for its mouse homolog remain unreported. In this study, we present the first crystal structure of mouse DYRK1A (mDYRK1A) encompassing residues 117-481 at a resolution of 3.0 Å. The crystallographic analysis revealed high conservation between mDYRK1A and human DYRK1A (hDYRK1A), with a 99% sequence identity, but identified a distinct structural variation attributable to a single amino acid substitution (S404 in mDYRK1A versus N404 in hDYRK1A). This substitution influences hydrogen bonding and tertiary structure, particularly within the CMGC-specific insertion region. Our findings underscore the importance of this residue in modulating structural stability and crystal packing. This study provides valuable insights into structural dynamics of DYRK1A and lays the groundwork for future studies on functional implications in mouse models of human diseases.

목차

INTRODUCTION

MATERIALS AND METHODS

RESULTS AND DISCUSSION

ACKNOWLEDGEMENTS

CONFLICT OF INTEREST

REFERENCES