Research

Research topics

Protein Structure Determination

The department Structural and Medicinal Biochemistry focuses on the elucidation of protein-protein and protein-ligand interactions using biochemical and biophysical strategies in addition to NMR as the main tool for the structure determination of biomolecules. Our research is geared towards predominantly human enzymes/proteins and their macromolecular complexes involved in posttranslational modification processes.

Biochemical Characterisation of Parvulins

Our focus in biochemistry and molecular biology is on parvulin type peptidyl-prolyl cis/trans isomerases (PPIases). The human genome encodes two of these proteins: Pin1 binds to and isomerizes phosphorylated Ser/Thr-Pro motifs and thus influences activity, localization and quality control of phosphorylated proteins. Par14 and its isoform Par17 are implicated in nuclear functions such as chromatin remodeling or RNA processing, in the regulation of receptor-mediated pathways (Par14) as well as in cytoskeleton organization and mitochondrial events (Par17). In addition to these representatives, we are interested in the function and biochemistry of parvulins of unicellular human parasites such as trypanosomes.

Biophysical studies on the interaction of synthetic supramolecular ligands and proteins

In collaboration with research groups from Chemistry, we are currently working on the interaction between proteins and supramolecular ligands such as organic tweezers and branched short polymers. Our interest is to understand and characterize the determinants of binding. With this knowledge, we aim to design proper synthetic ligands suitable for disrupting, stabilizing or modulating protein-protein-interactions.

Consortia

Entries in the Protein Database (PDB) - NMR

2N84

Solution structure of the FHA domain of TbPar42

Rehic E, Hoenig D, Kamba BE, Goehring A, Hofmann E, Gasper R, Matena A, Bayer P.(2019) Biomolecules 7;9(3).

RCSB PDB Entry

2N87

Solution structure of the PPIase domain of TbPar42

Rehic E, Hoenig D, Kamba BE, Goehring A, Hofmann E, Gasper R, Matena A, Bayer P.(2019) Biomolecules 7;9(3).

RCSB PDB Entry

2M08

The solution structure of NmPin, the parvuline of Nitrosopumilus maritimus

Hoppstock L, Trusch F, Lederer C, van West P, Koenneke M, Bayer P. (2016) Bmc Biol. 14: 53-53.

RCSB PDB Entry

2FNF

C1 domain of Nore1

Harjes E, Harjes S, Wohlgemuth S, Müller KH, Krieger E, Herrmann C, Bayer P. (2006) Structure 14: 881-888.

RCSB PDB Entry

2RQS

3D structure of Pin from the psychrophilic archeon Cenarcheaum symbiosum (CsPin)

Jaremko Ł, Jaremko M, Elfaki I, Mueller JW, Ejchart A, Bayer P, Zhukov I. J. Biol.Chem. 286: 6554-6565.

RCSB PDB Entry

2K76

Solution structure of a paralog-specific Mena binder by NMR

Link NM, Hunke C, Mueller JW, Eichler J, Bayer P. (2009) Biol.Chem. 390: 417-426.

RCSB PDB Entry

1A5R

Structure determination of the small Ubiquitin-related modifier Sumo-1, NMR, 10 Structures

Bayer P, Arndt A, Metzger S, Mahajan R, Melchior F, Jaenicke R, Becker J. (1998) J. Mol.Biol. 280: 275-286.

RCSB PDB Entry

1EQ3

NMR Structure of Human Parvulin HPAR14

Sekerina E, Rahfeld JU, Müller J, Fanghänel J, Rascher C, Fischer G, Bayer P. (2000)  J.Mol.Biol. 301: 1003-1017.

RCSB PDB Entry

1RLF

Structure determination of the RAS-binding domain of the RAL-specific guanine nucleotide exchange factor RLF

Esser D, Bauer B, Wolthuis RM, Wittinghofer A, Cool RH, Bayer P. (1998) Biochemistry 37: 13453-13462.

RCSB PDB Entry

1N3G

Solution structure of the ribosome-associated cold shock response protein Yfia of Escherichia coli

Rak A, Kalinin A, Shcherbakov D, Bayer P. (2002) Biochem. Biophys.Res.Commun. 299: 710-714.

RCSB PDB Entry

1NMW

Solution structure of the PPIase domain of human Pin1

Bayer E, Goettsch S, Mueller JW, Griewel B, Guiberman E, Mayr LM, Bayer P. (2003) J. Biol. Chem. 278: 26183-26193.

RCSB PDB Entry

1NMV

Solution structure of human Pin1

Bayer E, Goettsch S, Mueller JW, Griewel B, Guiberman E, Mayr LM, Bayer P. (2003) J. Biol. Chem. 278: 26183-26193.

RCSB PDB Entry

1RFH

Solution structure of the C1 domain of Nore1, a novel Ras effector

Harjes E, Harjes S, Wohlgemuth S, Müller KH, Krieger E, Herrmann C, Bayer P. (2006) Structure. 14(5):881-8.

RCSB PDB Entry

Entries in the Protein Database (PDB) - X-Ray

6GMP

Crystal Structure of the PPIASE Domain of TBPAR42

Rehic E, Hoenig D, Kamba BE, Goehring A, Hofmann E, Gasper R, Matena A, Bayer P. Biomolecules. 2019 7;9(3).

RCSB PDB Entry

3UI4

0.8 A resolution crystal structure of human Parvulin 14

Mueller JW, Link NM, Matena A, Hoppstock L, Rüppel A, Bayer P, Blankenfeldt W. (2011) J. Am. Chem. Soc. 133: 20096-20099.

RCSB PDB Entry

3UI5

Crystal structure of human Parvulin 14

Mueller JW, Link NM, Matena A, Hoppstock L, Rüppel A, Bayer P, Blankenfeldt W. J. Am. Chem. Soc. 133: 20096-20099.

RCSB PDB Entry

3UI6

0.89 A resolution crystal structure of human Parvulin 14 in complex with oxidized DTT

Mueller JW, Link NM, Matena A, Hoppstock L, Rüppel A, Bayer P, Blankenfeldt W. J. Am. Chem. Soc. 133: 20096-20099.

 

RCSB PDB Entry

1X6V

The crystal structure of human 3'-phosphoadenosine-5'-phosphosulfate synthetase 1

Harjes S, Bayer P, Scheidig AJ. (2005) J. Mol. Biol. 347: 623-635.

RCSB PDB Entry

1XJQ

ADP Complex OF HUMAN PAPS SYNTHETASE 1

Harjes S, Bayer P, Scheidig AJ. (2005)  J. Mol. Biol. 347: 623-635.

RCSB PDB Entry

1XNJ

APS complex of human PAPS synthetase 1

Harjes S, Bayer P, Scheidig AJ. (2005)  J. Mol. Biol. 347: 623-635.

RCSB PDB Entry

BMRB Data Bank:

BMRB-11080
BMRB-15946
BMRB-ID 4768
BMRB-ID 4768
BMRB-ID 5979
BMRB-ID 5979
BMRB-ID 6059
BMRB-ID 6059

The network bio-N3MR is a local association of research groups from North Rhine-Westphalia that employ nuclear magnetic resonance (NMR) spectroscopy to study biological macromolecules. The home page of a member group can be reached by clicking on the map.

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