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Muñoz, J.A.; ́mez, C. Go; Ballester, A.; ́zquez, M. L. Bla; ́lez, F. Gonza; Figueroa, M.

doi:10.1023/a:1003245701307

Cited by 63 publications

(15 citation statements)

References 5 publications

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“…The substantial di¡erence in helical content between these two regions is probably due to di¡erences in sequence composition. Indeed, residues 120^129 are predicted to populate helical conformations to a much greater extent than residues 134^144 by the program AGADIR, which predicts the helical behavior of peptides in solution [18].…”

Section: Resultsmentioning

confidence: 99%

Conformational preferences in the Ser¹³³‐phosphorylated and non‐phosphorylated forms of the kinase inducible transactivation domain of CREB

Radhakrishnan¹,

Pérez-Alvarado²,

Dyson³

et al. 1998

FEBS Letters

141

166

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Phosphorylation of SerIQQ within the kinase inducible transactivation domain (KID) of the transcription factor CREB potentiates interaction with the KIX domain of coactivator CBP. Heteronuclear NMR spectroscopic analyses reveal that the KID domain is largely unstructured except for residues that comprise the K KA helix in the pKID-KIX complex, which populate helical conformations to a significant extent ( s 50%). The helical content in the K KB region is very small in the non-phosphorylated form (V10%) although a small increase is detected upon Ser IQQ phosphorylation. The intrinsic bias towards helical conformations probably facilitates folding of the KID domain upon binding to KIX while the principal role of the phosphate group appears to be largely in mediating the intermolecular interactions in the pKID-KIX complex.z 1998 Federation of European Biochemical Societies.

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Section: Resultsmentioning

confidence: 99%

Conformational preferences in the Ser¹³³‐phosphorylated and non‐phosphorylated forms of the kinase inducible transactivation domain of CREB

Radhakrishnan¹,

Pérez-Alvarado²,

Dyson³

et al. 1998

FEBS Letters

141

166

View full text Add to dashboard Cite

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“…Structural models were obtained using Insight II Discover software from Biosym Technologies (San Diego, CA, USA), running on a Silicon Graphics Octane RS10000 Workstation. Models were built by the Biopolymer module of Insight II on the basis of the amino acid sequence propensity to form K-helix, random coil and L-sheet structures, as determined by the programs Agadir [12] and Gor IV [13] in the Expert Protein Analysis System (ExPASy) website (http://www.expasy.ch/www/tools.html). The structures were energy minimized using the Discover force ¢eld.…”

Section: Synthesis and Modelling Of Peptidesmentioning

confidence: 99%

“…4) recapitulates the main ¢nd- ings of this study and provides a structural framework to rationalize the activity (or lack thereof) of native and mutant peptides. To construct the model, we used two di¡erent algorithms (Agadir [12] and Gor IV [13], see Section 2) that predict helix/coil/L-sheet transitions and short range interactions in monomeric peptides under de¢ned conditions of pH, temperature and ionic strength. In small and highly hydrophilic peptides such as peptides Ske and Car, this is relatively straightforward and, indeed, both algorithms yielded essentially identical results.…”

Section: Structural Models Of the Skeletal And Cardiac Ii-iii Loopmentioning

confidence: 99%

Conversion of an inactive cardiac dihydropyridine receptor II‐III loop segment into forms that activate skeletal ryanodine receptors

et al. 1999

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A 25 amino acid segment (Glu 666^P ro 691 ) of the II-III loop of the K K 1 subunit of the skeletal dihydropyridine receptor, but not the corresponding cardiac segment (Asp 788^P ro 814 ), activates skeletal ryanodine receptors. To identify the structural domains responsible for activation of skeletal ryanodine receptors, we systematically replaced amino acids of the cardiac II-III loop with their skeletal counterparts. A cluster of five basic residues of the skeletal II-III loop ( 681 RKRRK 685 ) was indispensable for activation of skeletal ryanodine receptors. In the cardiac segment, a negatively charged residue (Glu 804 ) appears to diminish the electrostatic potential created by this basic cluster. In addition, Glu 800 in the group of negatively charged residues 798 EEEEE 802 of the cardiac II-III loop may serve to prevent the binding of the activation domain.z 1999 Federation of European Biochemical Societies.

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“…The reluctance of natural proteins to use helical side chain/side chain interactions as an important source of conformational stability might simply re£ect the inconvenience of this particular approach. In this respect it has been suggested that fast protein folding requires a predominance of non-local interactions [34,35] and that local interactions have a low speci¢city for the native state [36].…”

Section: How Protein K-helices Attain Stabilitymentioning

confidence: 99%

Intrahelical side chain interactions in α‐helices: poor correlation between energetics and frequency

Fernández‐Recio

Sancho

1998

FEBS Letters

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Polypeptide sequences in proteins may increase their tendency to adopt helical conformations in several ways. One is the recruiting of amino acid residues with high helical propensity. Another is the appropriate distribution of residues along the helix to establish stabilising side chain interactions. The first strategy is known to be followed by natural proteins because amino acids with high helical propensity are more frequent in K K-helices. If proteins also followed the second strategy, stabilising amino acid pairs should be more frequent than others. To test this possibility we compared empirical energies of side chain interactions in K K-helices with statistical energies calculated from a data base of proteins with low homology. We find some correlation between the stability afforded by the pairs and their relative abundance in K K-helices but the realisation of energetic preferences into statistical preferences is very low. This indicates that natural K K-helices do not regularly use intrahelical side chain interactions to increase their stability.z 1998 Federation of European Biochemical Societies.

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Cited by 63 publications

References 5 publications

Conformational preferences in the Ser¹³³‐phosphorylated and non‐phosphorylated forms of the kinase inducible transactivation domain of CREB

Conformational preferences in the Ser¹³³‐phosphorylated and non‐phosphorylated forms of the kinase inducible transactivation domain of CREB

Conversion of an inactive cardiac dihydropyridine receptor II‐III loop segment into forms that activate skeletal ryanodine receptors

Intrahelical side chain interactions in α‐helices: poor correlation between energetics and frequency

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Untitled

Cited by 63 publications

References 5 publications

Conformational preferences in the Ser133‐phosphorylated and non‐phosphorylated forms of the kinase inducible transactivation domain of CREB

Conformational preferences in the Ser133‐phosphorylated and non‐phosphorylated forms of the kinase inducible transactivation domain of CREB

Conversion of an inactive cardiac dihydropyridine receptor II‐III loop segment into forms that activate skeletal ryanodine receptors

Intrahelical side chain interactions in α‐helices: poor correlation between energetics and frequency

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Conformational preferences in the Ser¹³³‐phosphorylated and non‐phosphorylated forms of the kinase inducible transactivation domain of CREB

Conformational preferences in the Ser¹³³‐phosphorylated and non‐phosphorylated forms of the kinase inducible transactivation domain of CREB