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High-pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS. A conformational switch in RalGDS revealed from non-linear pressure shifts

Inoue, K. and Maurer, T. and Yamada, H. and Herrmann, C. and Horn, G. and Kalbitzer, Hans Robert and Akasaka, K. (2001) High-pressure NMR study of the complex of a GTPase Rap1A with its effector RalGDS. A conformational switch in RalGDS revealed from non-linear pressure shifts. FEBS letters 506 (3), pp. 180-184.

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Abstract

Unusually large non-linear 1H and 15N nuclear magnetic resonance chemical shifts against pressure have been detected for individual amide groups of the Ras-binding domain of Ral guanine dissociation stimulator (GDS). The non-linear response is largest in the region of the protein remote from the Rap1A-binding site, which increases by about two-fold by the complex formation with its effector ...

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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
11602241PubMed ID
Classification:
NotationType
Models, MolecularMESH
Nuclear Magnetic Resonance, Biomolecular/methodsMESH
PressureMESH
Signal TransductionMESH
ral Guanine Nucleotide Exchange Factor/chemistryMESH
rap1 GTP-Binding Proteins/chemistryMESH
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 09:08
Last Modified:15 Sep 2010 09:08
Item ID:16578
Owner Only: item control page
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