CSSB-EMBL

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2019-10-02
15:01
[PUBDB-2019-03581] Journal Article
et al
Molecular Organization of Soluble Type III Secretion System Sorting Platform Complexes
Many medically relevant Gram‐negative bacteria use the type III secretion system (T3SS) to translocate effector proteins into the host for their invasion and intracellular survival. A multi-protein complex located at the cytosolic interface of the T3SS is proposed to act as a sorting platform by selecting and targeting substrates for secretion through the system. [...]
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ddc:610
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2019-10-02
12:04
[PUBDB-2019-03563] Journal Article
et al
cGAS facilitates sensing of extracellular cyclic dinucleotides to activate innate immunity
EMBO reports 20(4), e46293 () [10.15252/embr.201846293]  GO
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ddc:570
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2019-09-30
12:26
[PUBDB-2019-03517] Journal Article
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Structure of Prototypic Peptide Transporter DtpA from E. coli in Complex with Valganciclovir Provides Insights into Drug Binding of Human PepT1
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ddc:540
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2018-12-17
14:21
[PUBDB-2018-05607] Abstract
et al
Membrane protein scaffold systems and SAXS characterization
iNEXT Annual Users Meeting, ESRFESRF, France, 19 Mar 2018 - 21 Mar 20182018-03-192018-03-21
Infrastructure needed for the solution characterization of reconstituted membrane proteins (MPs) has been designed and implemented at the iNEXT partner synchrotron facilities Petra-III (P12, EMBL-HH) and SOLEIL (SWING, SOLEIL). HT-SEC-SAXS systems are now optimized for purification and screening and rapid structural data collection of MPs. [...]
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2018-10-22
14:31
OpenAccess [PUBDB-2018-03874] Journal Article
et al
Saposin Lipid Nanoparticles: A Highly Versatile and Modular Tool for Membrane Protein Research
Structure 26(2), 345 - 355 () [10.1016/j.str.2018.01.007]  GO
Saposin-derived lipid nanoparticles (SapNPs) are a new alternative tool for membrane protein reconstitution. Here we demonstrate the potential and advantages of SapNPs [...]
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ddc:540
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2018-10-22
14:28
OpenAccess [PUBDB-2018-03873] Journal Article
et al
Multispecific Substrate Recognition in a Proton-Dependent Oligopeptide Transporter
Structure 26(3), 467 - 476 () [10.1016/j.str.2018.01.005]  GO
roton-dependent oligopeptide transporters (POTs) are important for uptake of dietary di- and tripeptides in many organisms, and in humans are also involved in drug absorption. These transporters accept a wide range of substrates, but the structural basis for how different peptide side chains are accommodated has so far remained obscure [...]
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ddc:540
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2018-10-22
13:46
OpenAccess [PUBDB-2018-03872] Journal Article

Tripeptide binding in a proton-dependent oligopeptide transporter
FEBS letters 592(19), 3239 - 3247 () [10.1002/1873-3468.13246]  GO
Proton‐dependent oligopeptide transporters (POTs) are important for the uptake of di‐/tripeptides in many organisms and for drug transport in humans. The binding mode of dipeptides has been well described [...]
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ddc:610
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2018-10-22
13:44
[PUBDB-2018-03870] Journal Article
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Probing the Architecture of a Multi-PDZ Domain Protein: Structure of PDZK1 in Solution
Structure 26(11), 1522 - 1533 () [10.1016/j.str.2018.07.016]  GO
The scaffolding protein PDZK1 has been associated with the regulation of membrane transporters. It contains four conserved PDZ domains, which typically recognize a 3–5-residue long motif at the C terminus of the binding partner. [...]
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2017-12-14
15:03
OpenAccess [PUBDB-2017-13499] Journal Article
et al
Lipid-like Peptides can Stabilize Integral Membrane Proteins for Biophysical and Structural Studies
ChemBioChem 18(17), 1735 - 1742 () [10.1002/cbic.201700235]  GO
A crucial bottleneck in membrane protein structural biology is the difficulty in identifying a detergent that can maintain the stability and functionality of integral membrane proteins (IMPs). Detergents are poor membrane mimics, and their common use in membrane protein crystallography may be one reason for the challenges in obtaining high-resolution crystal structures of many IMP families. [...]
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