seegerlab

RESEARCH GROUP SEEGER

RESEARCH GROUP SEEGER

university of zurich

RESEARCH GROUP SEEGER

RESEARCH GROUP SEEGER

university of zurich

RESEARCH GROUP SEEGER

RESEARCH GROUP SEEGER

university of zurich

RESEARCH GROUP SEEGER

RESEARCH GROUP SEEGER

university of zurich

RESEARCH GROUP SEEGER

RESEARCH GROUP SEEGER

university of zurich

RESEARCH GROUP SEEGER

RESEARCH GROUP SEEGER

university of zurich

RESEARCH GROUP SEEGER

RESEARCH GROUP SEEGER

university of zurich

RESEARCH GROUP SEEGER

RESEARCH GROUP SEEGER

university of zurich

our projects

MycoTransport

DrugEfflux

Sybodies

NestLink

Our mission

We are a team of creative, ambitious and friendly researchers who investigate membrane transport processes in pathogenic bacteria and develop innovative protein engineering tools. We combine the disciplines of structural biology, binder generation, protein biochemistry and microbiology to uncover molecular details of how membrane transport proteins expel antibiotics, shuttle siderophores and export lipids. Sybodies and NestLink enable us to target membrane transporters in the cellular context to develop rapid diagnostics, novel antibiotics and tailor-made research tools.

Interested to know more about our ups and downs with GlyT1? Read the brief behind the paper piece 👇

https://t.co/NL5OvW4ryy

@PoulNissen @seegerlab
@dandrite @MolBiolAU @EMBLHamburg @embl @Roche & LinksterTX

An ABC transporter wearing a crooked bow tie! 🤵Beautiful work by Jochen Zimmer's lab @MedicineUVA on O antigen transport required for LPS production in gram-negative bacteria! A dimeric carbohydrate binding domain binds to one NBD with striking asymmetry:
https://t.co/uGvHQmE523

Don't miss the talk of Prof. Dr. Kaspar Locher at Frontiers in Medicinal Chemistry 2021:
Structural studies of substrate and inhibitor binding to multidrug transporters by cryo-electron microscopy.
Mar 10, 10:45 a.m. UTC+1
Register: https://t.co/qEp3HohR0m
@lab_locher #CryoEM https://t.co/FNZvti7fPR
seegerlab photo

Agonist-bound OX2R cryo-EM structure in complex with a conformation-specific sybody👏
https://t.co/D5QrsjpGM6
We are proud to have contributed to this seminal study of Kaspar Hollenstein from @Merck by generating a conformation-selective high-affinity (600 pM) sybody💪

A beautiful start into the day! Sunrise view from our rooftop🌄☕️ https://t.co/JK8kEQs6n8 seegerlab photo