KESYSVYVYKV로부터 변형된 펩타이드 기질을 이용한 항바이러스제의 타깃이 되는 UL97 단백질 인산화 효소의 기질 특이성

• 영문명: Substrate Specificity of Protein Kinase UL97, an antiviral target, on Mutant Peptide Substrates Derived from a Peptide, KESYSVYVYKV
• 발행기관: 대한약학회
• 저자명: 백문창(Moon-Chang Baek)
• 간행물 정보: 『약학회지』제52권 제6호 (2008년), 466~470쪽, 전체 5쪽
• 주제분류: 의약학 > 기타의약학
• 파일형태: PDF
• 발행일자: 2008.12.31

영문 초록

Human cytomegalovirus expresses an unusual protein kinase UL97, a member of HVUL family of protein kinase. UL97 can phosphorylate nucleoside analogs such as ganciclovir as well as protein/peptide. It has previously been reported that UL97 is able to phosphorylate a KESYSVYVYKV peptide and that P+5 position (K) is important. We examined the extent of contribution of other positions (P-4 through P+6) of the peptide to be substrate of UL97 using alanine substituted peptides (Ala scanning) and deleted peptides. The result suggested that the E (P-2) is negative effect and P+5 (K) is still important. The peptide YSVYVYK is the shortest substrate enough to show high activity, which could be a starting point to develop peptidomimetic drug. This study would give important information to deeply understand the substrate specificity of UL97 and develop an antiviral drug using the small peptide identified here.

키워드

alanine scanning deleted peptide protein kinase UL97