The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors.
about
Structure, function, and evolution of bacterial ATP-binding cassette systemsEvolutionary relationships among G protein-coupled receptors using a clustered database approachSequence co-evolutionary information is a natural partner to minimally-frustrated models of biomolecular dynamicsThe conserved Candida albicans CA3427 gene product defines a new family of proteins exhibiting the generic periplasmic binding protein structural foldCrystal structure of a histidine kinase sensor domain with similarity to periplasmic binding proteinsConformational changes of glucose/galactose-binding protein illuminated by open, unliganded, and ultra-high-resolution ligand-bound structuresStructure-function relationships in a bacterial DING proteinStructural similarities between thiamin-binding protein and thiaminase-I suggest a common ancestorStructure-based design of a periplasmic binding protein antagonist that prevents domain closureDynamics and allosteric potential of the AMPA receptor N-terminal domainCrystallographic and microcalorimetric analyses reveal the structural basis for high arginine specificity in the Salmonella enterica serovar Typhimurium periplasmic binding protein STM4351Structures of the Escherichia coli transcription activator and regulator of diauxie, XylR: an AraC DNA-binding family member with a LacI/GalR ligand-binding domainEvidence for an allosteric mechanism of substrate release from membrane-transporter accessory binding proteinsEvidence for an ABC-Type Riboflavin Transporter System in Pathogenic Spirochetesmyo-Inositol and D-Ribose Ligand Discrimination in an ABC Periplasmic Binding ProteinRole of the Two Structural Domains from the Periplasmic Escherichia coli Histidine-binding Protein HisJSequence, biophysical, and structural analyses of the PstS lipoprotein (BB0215) fromBorrelia burgdorferireveal a likely binding component of an ABC-type phosphate transporterMolecular and structural basis of glutathione import in Gram-positive bacteria via GshT and the cystine ABC importer TcyBC of Streptococcus mutansImperfect coordination chemistry facilitates metal ion release in the Psa permeaseCrystal structure of the phosphate-binding protein (PBP-1) of an ABC-type phosphate transporter from Clostridium perfringensThe 1.1 Å resolution structure of a periplasmic phosphate-binding protein from Stenotrophomonas maltophilia: a crystallization contaminant identified by molecular replacement using the entire Protein Data BankConformational transitions upon ligand binding: holo-structure prediction from apo conformationsEvolution of the class C GPCR Venus flytrap modules involved positive selected functional divergenceMolecular dynamics simulations reveal that apo-HisJ can sample a closed conformation.The solution structure, binding properties, and dynamics of the bacterial siderophore-binding protein FepBTorT, a member of a new periplasmic binding protein family, triggers induction of the Tor respiratory system upon trimethylamine N-oxide electron-acceptor binding in Escherichia coli.Mining the gene repertoire and ESTs for G protein-coupled receptors with evolutionary perspective.GrlJ, a Dictyostelium GABAB-like receptor with roles in post-aggregation developmentMolecular evolution of the two-component system BvgAS involved in virulence regulation in BordetellaEnhancing UCSF Chimera through web servicesAccessing a hidden conformation of the maltose binding protein using accelerated molecular dynamicsSolution NMR studies of periplasmic binding proteins and their interaction partnersCalcium-sensing receptor biosynthesis includes a cotranslational conformational checkpoint and endoplasmic reticulum retentionInsect stage-specific receptor adenylate cyclases are localized to distinct subdomains of the Trypanosoma brucei Flagellar membrane.Characterization of a truncated metabotropic glutamate receptor in a primitive metazoan, the parasitic flatworm Schistosoma mansoniRab1 small GTP-binding protein regulates cell surface trafficking of the human calcium-sensing receptor.Exploration of multi-state conformational dynamics and underlying global functional landscape of maltose binding protein.Change in rigidity in the activated form of the glucose/galactose receptor from Escherichia coli: a phenomenon that will be key to the development of biosensors.Genetic variations in human G protein-coupled receptors: implications for drug therapy.The hybrid histidine kinase Hk1 is part of a two-component system that is essential for survival of Borrelia burgdorferi in feeding Ixodes scapularis ticks
P2860
Q24643436-5DD8B087-5FB2-426F-B7D6-044B68E245FEQ24654262-A395D9D1-9696-4ACC-A4FA-C492313A5D65Q26766142-10FBABDA-2B75-4530-889C-95B2843082D8Q27348287-CA5B10A4-52C4-47FA-92CB-99637E33225EQ27643947-1A865C31-92EA-4646-8D3A-84D2B20D6587Q27644665-BA83626F-5AED-4C02-99F0-43FC86534C3DQ27646564-6A585577-E06E-4487-90EE-1FC2008C6BCAQ27649481-60504340-2F06-4D09-8DC9-249925A67C26Q27654562-5FEF0B80-E121-4235-BD85-5606AA0BF7D1Q27666952-1DFFB1FE-CA53-4E86-A55C-8D0BAA90A791Q27667788-AEF0D6AD-239C-4976-9CC6-2634954480B7Q27675506-7CE0B558-0AE8-4BC6-8EC1-EFBDACE0E733Q27675569-DF6A13EA-55E6-49DE-A836-7C8C0D25E8DCQ27676350-B0DFCF78-50F0-4211-A1F1-14FC9D054AEEQ27676855-F7FB69E0-02F1-426A-82D5-724DE448A5DEQ27679943-8CC3E8A2-75CA-4413-9D38-3115A361417AQ27680836-237FEE89-B914-4C7C-8410-54EF5055C584Q27684685-62725721-62D2-4BF8-BC1B-F88929B95349Q27687486-BD8B76F4-7AF4-4018-BCEF-F33925AA0855Q27695725-B1576092-AB5B-41A0-944B-33A37C93CD3CQ27724447-F83D13D1-5481-4998-826F-6A7AEAA47320Q28472382-0086A770-E69E-49F3-9E3C-8B91DFF5C9A6Q28754701-92DAA1E9-D9DC-4525-AAA7-65A1A8437126Q30353042-A6F36D55-49BF-41F6-BEE6-FCE0C4B49115Q30366264-EA70C534-AEFD-4DCD-BED2-1AB33DB99FD7Q31066812-F7F3536F-B16A-415E-B362-8882220F21ACQ33281813-A4D098AB-CFD5-47DE-8B5B-6C53D4C043A5Q33284566-F9BDDC34-9C4D-41FF-9808-F3E6CF864327Q33502712-9DB4A900-DD4F-430E-8E32-69A589D51CCDQ33860839-636A5D1B-EBD0-4D7E-B27C-FB7E2096CB05Q33886144-8B68FB53-DDB4-481E-A942-8C3B6D6D678AQ33896675-EC9C3017-DEC7-47EF-93AF-47F1A40FE29BQ33924278-EF8FD6C3-E676-4420-8EB3-29DBC2CD039DQ34057290-BFE3C143-74BF-4A35-ABE2-E5E209E4089EQ34070596-28A9C0ED-5C64-4DEE-9C48-C1B6EA08F971Q34197779-7EF2ADCC-E02E-40B0-A1FC-1A213A3C1BE7Q34244861-187C01A3-9EC5-40EF-BB63-47793FAF0A87Q34353110-83D5E751-11D7-4CF3-8CDE-270C5F1AB628Q34461998-ED3DE0CA-917A-4EB5-ABE6-5293892B4A97Q35139218-A8EB7363-47A4-4D38-ADA3-111D9F15DDC5
P2860
The Venus flytrap of periplasmic binding proteins: an ancient protein module present in multiple drug receptors.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@ast
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@en
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@nl
type
label
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@ast
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@en
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@nl
prefLabel
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@ast
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@en
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@nl
P2093
P2860
P356
P1433
P1476
The Venus flytrap of periplasm ...... nt in multiple drug receptors.
@en
P2093
P2860
P356
10.1208/PS010202
P577
1999-01-01T00:00:00Z