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钙调素的分子识别研究进展 被引量:9

Progress in molecular recognition of calmodulin
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摘要 钙调素 (CaM ) ,作为细胞内Ca2 + 信号传导途径中的主要信号转导分子 ,普遍存在于真核细胞中 ,介导调控由Ca2 + 引起的一系列生理生化反应 ,参与并调节细胞的增生、分化、运动等基本代谢过程。对CaM的结构及分子识别机制的研究 ,有助于更好地理解细胞信号传导、蛋白质相互作用的分子机制 ,对新药开发和临床治疗具有重要的指导意义。本文作者就近几年来有关CaM结构及分子识别机制的研究现状作一概述。 Calmodulin(CaM),as major intracellular Ca 2+ signal transductor,is a ubiquitous, multifunctional protein in eukaryotic cells,invovled in a wide variety of cellular processes . Study of the structure and molecular recognition mechanism of CaM helps better understanding intracellular Ca 2+ signaling system and molecular recognition of protein-protein interaction,giving new insight into medicine development and clinical therapy. This paper reviews progress in the studies of molecular recognition of calmodulin in recent past years.
出处 《医学研究生学报》 CAS 2003年第11期846-849,共4页 Journal of Medical Postgraduates
基金 江苏省自然科学基金资助项目 (批准号 :BK95 14 13 0 7)
关键词 钙调素 分子识别 钙调素结合蛋白 基序 Calmodulin Molecular recognition Calmodulin binding proteins Motif
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  • 1Vogel HJ. Calmodulin: a versatile calcium mediator protein[J].Biochem Cell Biol,1994,72(9): 357-376.
  • 2Crivici A,Ikura M. Molecular and structural basis of target recognition by calmodulin[J]. Annu Rev Biophys Biomol Struct,1995,24: 85-116.
  • 3Gonda K,Komatsu M,Numata O. Calmodulin and Ca2+/calmodulin-binding proteins are involved in tetrahymena thermophila phagocytosis[J].Cell Struct Funct,2000,25(4):243-251.
  • 4Laoudj D,Andersen CL,Bras A et al. EGTA induces the synthesis in escherichia coli of three proteins that cross-react with calmodulin antibodies[J].Mol Microbiol,1994,13(3):445.
  • 5Luis AJ,Priya SC,Harry WJ. Apocalmodulin[J].Physiologic Revi,1999,79(3): 661-682.
  • 6Brenda RS,Laurel AF,Rainbo H et al. An interdomain linker increases the thermostability and decreases the calcium affinity of the calmodulin N-domain[J].Bochemistry,2002,41(1): 15-20.
  • 7Abdessamad A,Ryan AS,John RD. Long-range effects on calcium binding and conformational change in the N-domain of calmodulin[J]. Biochemistry,2001,40(42): 12719-12726.
  • 8Sandrine F,Rodolfo RB,John EM et al. Calcium-induced refolding of the calmodulin V136G mutant studied by NMR spectroscopy:evidence for interaction between the two globular domains[J].Biochemistry,2000,39(51): 15920-15931.
  • 9Hongye S,Dan Y,Laurel AC et al. Mutation of Tyr 138 disrupts the structural coupling between the opposing domains in vertebrate calmodulin[J].Biochemistry,2001,40(32):9605-9617.
  • 10Weljie AM,Yamniuk AP,Yoshino H et al. Protein conformational changes studied by diffusion NMR spectroscopy:Application to helix-loop-helix calcium binding proteins[J].Protein Sci,2003,12(2):228-236 .

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