Crystal structure of the HHD2 domain in human RTEL1

• 영문명: Crystal structure of the HHD2 domain in human RTEL1
• 발행기관: 한국구조생물학회
• 저자명: Inseop Chun Eunhye Jung Whan Jong Kim Min-Sung Kim
• 간행물 정보: 『Biodesign』Vol 12, No 1, Mar, 3~7쪽, 전체 5쪽
• 주제분류: 자연과학 > 생물학
• 파일형태: PDF
• 발행일자: 2024.03.30

영문 초록

The regulator of telomere elongation helicase 1 (RTEL1) is involved in maintaining telomere DNA, DNA repair, and genome stability through the disassembly of D-loops and unwinding G-quadruplex structures. RTEL1 consists of a helicase domain, two tandem harmonin homology domains (HHD1 and HHD2), and a Zn2+ binding RING domain. The HHD1 and HHD2 domains of RTEL1, each characterized by five α-helices, play roles in protein-protein interactions. HHD1 interacts with SLX4, a tumor suppressor protein associated with endonucleases. HHD2 interacts with Telomeric repeat-containing RNAs (TERRAs), and the 32C domain of RPA. Here, we present the crystal structure of the HHD2 domain from human RTEL1. The crystal of HHD2 domain belongs to the space group P21, with unit cell parameters a = 66.05, b = 61.96, and c = 79.95 Å. The structure was refined to a resolution of 2.8 Å with Rwork/Rfree = 23.9/26.83%.

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INTRODUCTION

RESULTS AND DISCUSSION

MATERIALS AND METHODS

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