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Literature DB >> 11504940

Propagating conformational changes over long (and short) distances in proteins.

Abstract

The problem of the propagation of conformational changes over long distances or through a closely packed protein is shown to fit a model of a ligand-induced conformational change between two protein states selected by evolution. Moreover, the kinetics of the pathway between these states is also selected so that the energy of ligand binding and the speed of the transition between conformational states are physiologically appropriate. The crystallographic data of a wild-type aspartate receptor that has negative cooperativity and a mutant that has no cooperativity but has native transmembrane signaling are shown to support this model.

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Year: 2001 PMID： 11504940 PMCID： PMC55484 DOI： 10.1073/pnas.161239298

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

11 in total

1. A piston model for transmembrane signaling of the aspartate receptor.

Authors: K M Ottemann; W Xiao; Y K Shin; D E Koshland
Journal: Science Date: 1999-09-10 Impact factor: 47.728

2. The structural basis of ribosome activity in peptide bond synthesis.

Authors: P Nissen; J Hansen; N Ban; P B Moore; T A Steitz
Journal: Science Date: 2000-08-11 Impact factor: 47.728

3. High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor.

Authors: J I Yeh; H P Biemann; G G Privé; J Pandit; D E Koshland; S H Kim
Journal: J Mol Biol Date: 1996-09-20 Impact factor: 5.469

4. Stereochemistry of cooperative effects in haemoglobin.

Authors: M F Perutz
Journal: Nature Date: 1970-11-21 Impact factor: 49.962

Review 5. Structural mechanisms for domain movements in proteins.

Authors: M Gerstein; A M Lesk; C Chothia
Journal: Biochemistry Date: 1994-06-07 Impact factor: 3.162

Review 6. Active and inactive protein kinases: structural basis for regulation.

Authors: L N Johnson; M E Noble; D J Owen
Journal: Cell Date: 1996-04-19 Impact factor: 41.582

7. Comparison of experimental binding data and theoretical models in proteins containing subunits.

Authors: D E Koshland; G Némethy; D Filmer
Journal: Biochemistry Date: 1966-01 Impact factor: 3.162

8. Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity.

Authors: H P Biemann; D E Koshland
Journal: Biochemistry Date: 1994-01-25 Impact factor: 3.162

9. Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium.

Authors: W G Scott; D L Milligan; M V Milburn; G G Privé; J Yeh; D E Koshland; S H Kim
Journal: J Mol Biol Date: 1993-07-20 Impact factor: 5.469

10. The fifth Datta Lecture. Structural similarities between the aspartate receptor of bacterial chemotaxis and the trp repressor of E. coli. Implications for transmembrane signaling.

Authors: B A Lynch; D E Koshland
Journal: FEBS Lett Date: 1992-07-27 Impact factor: 4.124

47 in total

Review 1. Ingestion-controlling network: what's language got to do with it?

Authors: Michael Myslobodsky; Richard Coppola
Journal: Rev Neurosci Date: 2010 Impact factor: 4.353

2. Crystal structure of the bromide-bound D85S mutant of bacteriorhodopsin: principles of ion pumping.

Authors: Marc T Facciotti; Vincent S Cheung; Doris Nguyen; Shahab Rouhani; Robert M Glaeser
Journal: Biophys J Date: 2003-07 Impact factor: 4.033

3. A possible degree of motional freedom in bacterial chemoreceptor cytoplasmic domains and its potential role in signal transduction.

Authors: Weiguo Hu
Journal: Int J Biochem Mol Biol Date: 2011-02-25

Propagating conformational changes over long (and short) distances in proteins.

1. A piston model for transmembrane signaling of the aspartate receptor.

2. The structural basis of ribosome activity in peptide bond synthesis.

3. High-resolution structures of the ligand binding domain of the wild-type bacterial aspartate receptor.

4. Stereochemistry of cooperative effects in haemoglobin.

Review 5. Structural mechanisms for domain movements in proteins.

Review 6. Active and inactive protein kinases: structural basis for regulation.

7. Comparison of experimental binding data and theoretical models in proteins containing subunits.

8. Aspartate receptors of Escherichia coli and Salmonella typhimurium bind ligand with negative and half-of-the-sites cooperativity.

9. Refined structures of the ligand-binding domain of the aspartate receptor from Salmonella typhimurium.

10. The fifth Datta Lecture. Structural similarities between the aspartate receptor of bacterial chemotaxis and the trp repressor of E. coli. Implications for transmembrane signaling.

Review 1. Ingestion-controlling network: what's language got to do with it?

2. Crystal structure of the bromide-bound D85S mutant of bacteriorhodopsin: principles of ion pumping.

3. A possible degree of motional freedom in bacterial chemoreceptor cytoplasmic domains and its potential role in signal transduction.

4. Mechanical response and conformational amplification in α-helical coiled coils.

Review 5. Solution NMR Spectroscopy for the Study of Enzyme Allostery.

6. Communication over the network of binary switches regulates the activation of A2A adenosine receptor.

7. Contact rearrangements form coupled networks from local motions in allosteric proteins.

8. Directed evolution of protein switches and their application to the creation of ligand-binding proteins.

Review 9. Describing sequence-ensemble relationships for intrinsically disordered proteins.

10. In situ D-periodic molecular structure of type II collagen.