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Nucleotide-binding characteristics of human guanylate-binding protein 1 (hGBP1) and identification of the third GTP-binding motif

Praefcke, G. J. and Geyer, M. and Schwemmle, M. and Kalbitzer, Hans Robert and Herrmann, C. (1999) Nucleotide-binding characteristics of human guanylate-binding protein 1 (hGBP1) and identification of the third GTP-binding motif. Journal of molecular biology 292 (2), pp. 321-332.

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Abstract

hGBP1 is a GTPase with antiviral activity encoded by an interferon- activated human gene. Specific binding of hGBP1 to guanine nucleotides has been established although only two classical GTP-binding motifs were found in its primary sequence. The unique position of hGBP1 amongst known GTPases is further demonstrated by the hydrolysis of GTP to GDP and GMP. Although subsequent cleavage of ...

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Item Type:Article
Date:1999
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
10493878PubMed ID
10.1006/jmbi.1999.3062DOI
Classification:
NotationType
5'-Guanylic Acid/metabolismMESH
Aluminum Compounds/chemistryMESH
Binding SitesMESH
Binding, CompetitiveMESH
CalorimetryMESH
DNA-Binding Proteins/chemistryMESH
Fluorides/chemistryMESH
FluorometryMESH
GTP-Binding ProteinsMESH
Guanosine Diphosphate/metabolismMESH
Guanosine Triphosphate/metabolismMESH
HumansMESH
KineticsMESH
Magnetic Resonance SpectroscopyMESH
MutationMESH
Recombinant Proteins/chemistryMESH
ThermodynamicsMESH
Subjects:500 Science > 570 Life sciences
Status:Published
Refereed:Unknown
Created at the University of Regensburg:Unknown
Owner: Gertraud Kellers
Deposited On:13 Sep 2010 07:59
Last Modified:13 Sep 2010 07:59
Item ID:16566
Owner Only: item control page
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