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Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe

Gronwald, W. and Huber, F. and Grünewald, P. and Spörner, M. and Wohlgemuth, S. and Herrmann, C. and Kalbitzer, Hans Robert (2001) Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe. Structure 9 (11), pp. 1029-1041.

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Abstract

BACKGROUND: After activation, small GTPases such as Ras transfer the incoming signal to effectors by specifically interacting with the binding domain of these proteins. Structural details of the binding domain of different effectors determine which pathway is predominantly activated. Byr2 from fission yeast is a functional homolog of Raf, which is the direct downstream target of Ras in mammalians ...

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Item Type:Article
Date:2001
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
11709167PubMed ID
Classification:
NotationType
Amino Acid SequenceMESH
Binding SitesMESH
Enzyme ActivationMESH
Fungal Proteins/metabolismMESH
Guanylyl Imidodiphosphate/chemistryMESH
MAP Kinase Kinase KinasesMESH
Mitogen-Activated Protein Kinases/metabolismMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Protein BindingMESH
Protein Structure, SecondaryMESH
Protein Structure, TertiaryMESH
Schizosaccharomyces/enzymologyMESH
Schizosaccharomyces pombe ProteinsMESH
Sequence Homology, Amino AcidMESH
ras Proteins/metabolismMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:15 Sep 2010 09:09
Last Modified:15 Sep 2010 09:09
Item ID:16579
Owner Only: item control page
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