Go to content
UR Home

Combining ancestral sequence reconstruction with protein design to identify an interface hotspot in a key metabolic enzyme complex

Holinski, Alexandra, Heyn, Kristina, Merkl, Rainer and Sterner, Reinhard (2017) Combining ancestral sequence reconstruction with protein design to identify an interface hotspot in a key metabolic enzyme complex. Proteins: Structure, Function, and Bioinformatics 85 (2), pp. 312-321.

Full text not available from this repository.

at publisher (via DOI)

Other URL: http://doi.org/10.1002/prot.25225


Abstract

It is important to identify hotspot residues that determine protein-protein interactions in interfaces of macromolecular complexes. We have applied a combination of ancestral sequence reconstruction and protein design to identify hotspots within imidazole glycerol phosphate synthase (ImGPS). ImGPS is a key metabolic enzyme complex, which links histidine and de novo purine biosynthesis and ...

plus


Export bibliographical data



Item type:Article
Date:2017
Institutions:Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Biochemie I
Identification Number:
ValueType
10.1002/prot.25225DOI
Keywords:GLYCEROL PHOSPHATE SYNTHASE; SITE-DIRECTED MUTAGENESIS; QUATERNARY STRUCTURE; CRYSTAL-STRUCTURE; BIENZYME COMPLEX; HOT-SPOT; EVOLUTION; PREDICTION; MUTATIONS; GLUTAMINE; HisF; HisH; imidazole glycerol phosphate synthase; in silico mutagenesis; protein-protein interaction
Dewey Decimal Classification:500 Science > 570 Life sciences
Status:Published
Refereed:Yes, this version has been refereed
Created at the University of Regensburg:Yes
Item ID:38737
Owner only: item control page
  1. Homepage UR

University Library

Publication Server

Contact:

Publishing: oa@ur.de

Dissertations: dissertationen@ur.de

Research data: daten@ur.de

Contact persons