Restructuring of the dinucleotide-binding fold in an NADP(H) sensor   protein

doi:10.1073/pnas.0700480104

CORC > 北京大学 > 生命科学学院

	Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein
	Zheng, Xiaofeng ; Dai, Xueyu ; Zhao, Yanmei ; Chen, Qiang ; Lu, Fei ; Yao, Deqiang ; Yu, Quan ; Liu, Xinping ; Zhang, Chuanmao ; Gu, Xiaocheng ; Luo, Ming
刊名	proceedings of the national academy of sciences of the united states of america
	2007
关键词	Rossmann fold signal transduction SACCHAROMYCES-CEREVISIAE CALORIE RESTRICTION NITRIC-OXIDE LIFE-SPAN GLUCOSE-6-PHOSPHATE-DEHYDROGENASE CELL EXPRESSION STRESS DEHYDROGENASE RESOLUTION
DOI	10.1073/pnas.0700480104
英文摘要	NAD(P) has long been known as an essential energy-carrying molecule in cells. Recent data, however, indicate that NAD(P) also plays critical signaling roles in regulating cellular functions. The crystal structure of a human protein, HSCARG, with functions previously unknown, has been determined to 2.4-angstrom resolution. The structure reveals that HSCARG can form an asymmetrical dinner with one subunit occupied by one NADP molecule and the other empty. Restructuring of its NAD(P)-binding Rossmann fold upon NADP binding changes an extended loop to an a-helix to restore the integrity of the Rossmann fold. The previously unobserved restructuring suggests that HISCARG may assume a resting state when the level of NADP(H) is normal within the cell. When the NADP(H) level passes a threshold, an extensive restructuring of HSCARG would result in the activation of its regulatory functions. Immunofluorescent imaging shows that HISCARG redistributes from being associated with intermediate filaments in the resting state to being dispersed in the nucleus and the cytoplasm. The structural change of HSCARG upon NADP(H) binding could be a new regulatory mechanism that responds only to a significant change of NADP(H) levels. One of the functions regulated by HSCARG may be argininosuccinate synthetase that is involved in NO synthesis.; http://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcApp=PARTNER_APP&SrcAuth=LinksAMR&KeyUT=WOS:000246853700025&DestLinkType=FullRecord&DestApp=ALL_WOS&UsrCustomerID=8e1609b174ce4e31116a60747a720701 ; Multidisciplinary Sciences; SCI(E); PubMed; 36; ARTICLE; 21; 8809-8814; 104
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/162629]
专题	生命科学学院
推荐引用方式 GB/T 7714	Zheng, Xiaofeng,Dai, Xueyu,Zhao, Yanmei,et al. Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein[J]. proceedings of the national academy of sciences of the united states of america,2007.
APA	Zheng, Xiaofeng.,Dai, Xueyu.,Zhao, Yanmei.,Chen, Qiang.,Lu, Fei.,...&Luo, Ming.(2007).Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein.proceedings of the national academy of sciences of the united states of america.
MLA	Zheng, Xiaofeng,et al."Restructuring of the dinucleotide-binding fold in an NADP(H) sensor protein".proceedings of the national academy of sciences of the united states of america (2007).