User:Meili Yang/sandbox 1: Difference between revisions
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One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | One of the [[CBI Molecules]] being studied in the [http://www.umass.edu/cbi/ University of Massachusetts Amherst Chemistry-Biology Interface Program] at UMass Amherst and on display at the [http://www.molecularplayground.org/ Molecular Playground]. | ||
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved. | The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved. | ||
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Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors. | Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors. | ||
''Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.'' | |||
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<applet load=' | <applet load='2ho9' size='[450,338]' frame='true' align='right' | ||
caption= 'Cytoplasmic domain of a serine chemotaxis receptor(1qu7)' scene='User:Meili_Yang/sandbox_1/Cytoplasmic_domain/1'> | caption='Cytoplasmic domain of a serine chemotaxis receptor(1qu7)' scene='User:Meili_Yang/sandbox_1/Cytoplasmic_domain/1'> | ||
The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor. | The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor. | ||
Latest revision as of 01:41, 10 December 2010
One of the CBI Molecules being studied in the University of Massachusetts Amherst Chemistry-Biology Interface Program at UMass Amherst and on display at the Molecular Playground.
The bacterial chemotaxis receptors are transmembrane receptors with a simple signalling pathway which has elements relevant to the general understanding of signal recognition and transduction across membranes, how signals are relayed between molecules in a pathway, and how adaptation to a persistent signal is achieved.
Bacterial chemotaxis receptors are composed of a ligand-binding domain, a transmembrane domain consisting of two helices TM1 and TM2, and a cytoplasmic domain. All known bacterial chemotaxis receptors have a highly conserved cytoplasmic domain, which unites signals from different ligand domains into a single signalling pathway to flagella motors.
Four-helical-bundle structure of the cytoplasmic domain of a serine chemotaxis receptor., Kim KK, Yokota H, Kim SH, Nature. 1999 Aug 19;400(6746):787-92.
Cytoplasmic domain of TSRCytoplasmic domain of TSR
<applet load='2ho9' size='[450,338]' frame='true' align='right' caption='Cytoplasmic domain of a serine chemotaxis receptor(1qu7)' scene='User:Meili_Yang/sandbox_1/Cytoplasmic_domain/1'>
The structure of the cytoplasmic domain of a serine chemotaxis receptor(TSR) of Escherichia coli is a 200 A-long coiled-coil of two antiparallel helices connected by a 'U-turn'. Two of these domains form a long, supercoiled, four-helical bundle in the cytoplasmic portion of the receptor.