인문학
사회과학
자연과학
공학
의약학
농수해양학
예술체육학
복합학
DBpia AI
AI 에이전트
AI 아이디어
AI 리더
AI 뷰어
Citeasy
크롬 서지관리 다운로드
지원사업
학술연구/단체지원/교육 등 연구자 활동을 지속하도록 DBpia가 지원하고 있어요.
커뮤니티
연구자들이 자신의 연구와 전문성을 널리 알리고, 새로운 협력의 기회를 만들 수 있는 네트워킹 공간이에요.
초록·키워드
The poliovirus nonstructural protein 3CD is composed of two domains named 3C and 3D, separated by a 7-8-residue linker.The N-terminal 3C domain possesses protease activity and the 3D protein alone is an RNA-dependent RNA polymerase (RdRp).Intriguingly, the 3CD precursor does not have RdRp function, but 3CD works as a better protease than 3C.Although the X-ray crystal structure of 3CD has been obtained, it cannot explicitly explain the higher protease activity of 3CD compared to 3C.According to previous molecular dynamics (MD) studies and verified by small-angle X-ray scattering experiments (SAXS), there are transient domaindomain interactions that may allow 3CD to adopt extended and compact conformations.To probe these potential 3C-3D interactions, we generated amino acid substitutions at key locations (i.e.D32A, K60A, K78A, S177A, and K531A) and characterized these protein variants using SAXS, Analytical Ultra Centrifugation (AUC), Dynamic Light Scattering (DLS), Circular Dichroism (CD) Spectroscopy and other biophysical techniques on 3CD proteins.Preliminary SAXS results, including changes to the radii of gyration (Rg) and solvent envelopes derived from DENSS, were consistent with variants favoring extended conformations.AUC also indicated changes to the frictional ratio, which would also be suggestive with a change to the conformational equilibrium.Altogether, these results provide compelling evidence that there are different conformations of the 3CD protein in solution.The 3CD conformations and 3C-3D domain interactions may contribute to the functional differences between 3CD and 3C/3D, which these variants may help to verify.
인공지능 문자 인식 모델을 통해 추출된 텍스트로, 일부 오타나 오류가 포함될 수 있으나 지속적으로 개선 중입니다.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
오류를 발견하셨다면 해당 부분을 드래그한 후 ' 를 통해 신고해주세요.
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