نتایج جستجو برای: binding pocket

تعداد نتایج: 429861  

Journal: :Genes & development 2012
Jason R Burke Greg L Hura Seth M Rubin

Cyclin-dependent kinase (Cdk) phosphorylation of the Retinoblastoma protein (Rb) drives cell proliferation through inhibition of Rb complexes with E2F transcription factors and other regulatory proteins. We present the first structures of phosphorylated Rb that reveal the mechanism of its inactivation. S608 phosphorylation orders a flexible "pocket" domain loop such that it mimics and directly ...

Journal: :Anesthesiology 2016
Monica N Kinde Weiming Bu Qiang Chen Yan Xu Roderic G Eckenhoff Pei Tang

BACKGROUND Identifying functionally relevant anesthetic-binding sites in pentameric ligand-gated ion channels (pLGICs) is an important step toward understanding the molecular mechanisms underlying anesthetic action. The anesthetic propofol is known to inhibit cation-conducting pLGICs, including a prokaryotic pLGIC from Erwinia chrysanthemi (ELIC), but the sites responsible for functional inhibi...

2012
Lianming Zhang Yiqing Chen Hau-San Wong Shuigeng Zhou Hiroshi Mamitsuka Shanfeng Zhu

MOTIVATION Accurate identification of peptides binding to specific Major Histocompatibility Complex Class II (MHC-II) molecules is of great importance for elucidating the underlying mechanism of immune recognition, as well as for developing effective epitope-based vaccines and promising immunotherapies for many severe diseases. Due to extreme polymorphism of MHC-II alleles and the high cost of ...

Journal: :Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 2012

2013
Christopher D. Wassman Roberta Baronio Özlem Demir Brad D. Wallentine Chiung-Kuang Chen Linda V. Hall Faezeh Salehi Da-Wei Lin Benjamin P. Chung G. Wesley Hatfield A. Richard Chamberlin Hartmut Luecke Richard H. Lathrop Peter Kaiser Rommie E. Amaro

The tumour suppressor p53 is the most frequently mutated gene in human cancer. Reactivation of mutant p53 by small molecules is an exciting potential cancer therapy. Although several compounds restore wild-type function to mutant p53, their binding sites and mechanisms of action are elusive. Here computational methods identify a transiently open binding pocket between loop L1 and sheet S3 of th...

Journal: :Science 2013
Chong Wang Yi Jiang Jinming Ma Huixian Wu Daniel Wacker Vsevolod Katritch Gye Won Han Wei Liu Xi-Ping Huang Eyal Vardy John D McCorvy Xiang Gao X Edward Zhou Karsten Melcher Chenghai Zhang Fang Bai Huaiyu Yang Linlin Yang Hualiang Jiang Bryan L Roth Vadim Cherezov Raymond C Stevens H Eric Xu

Serotonin or 5-hydroxytryptamine (5-HT) regulates a wide spectrum of human physiology through the 5-HT receptor family. We report the crystal structures of the human 5-HT1B G protein-coupled receptor bound to the agonist antimigraine medications ergotamine and dihydroergotamine. The structures reveal similar binding modes for these ligands, which occupy the orthosteric pocket and an extended bi...

Journal: :The Biochemical journal 2006
Tip W Loo M Claire Bartlett David M Clarke

P-gp (P-glycoprotein; ABCB1) protects us by transporting a broad range of structurally unrelated compounds out of the cell. Identifying the regions of P-gp that make up the drug-binding pocket is important for understanding the mechanism of transport. The common drug-binding pocket is at the interface between the transmembrane domains of the two homologous halves of P-gp. It has been shown in a...

Journal: :Proteins 2002
Suman Kundu Barry Snyder Kaustuv Das Pramit Chowdhury Jaehun Park Jacob W Petrich Mark S Hargrove

Sperm whale myoglobin (Mb) and soybean leghemoglobin (Lba) are two small, monomeric hemoglobins that share a common globin fold but differ widely in many other aspects. Lba has a much higher affinity for most ligands, and the two proteins use different distal and proximal heme pocket regulatory mechanisms to control ligand binding. Removal of the constraint provided by covalent attachment of th...

Journal: :The Journal of biological chemistry 2005
Caroline Silve Christophe Petrel Christine Leroy Henri Bruel Eric Mallet Didier Rognan Martial Ruat

The Ca(2+)-sensing receptor (CaSR) belongs to the class III G-protein-coupled receptors (GPCRs), which include receptors for pheromones, amino acids, sweeteners, and the neurotransmitters glutamate and gamma-aminobutyric acid (GABA). These receptors are characterized by a long extracellular amino-terminal domain called a Venus flytrap module (VFTM) containing the ligand binding pocket. To eluci...

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