TY  - JOUR
AB  - Amyloid fibrils from Alzheimer's amyloid-beta peptides (Aβ) are found to be polymorphic. So far, 14 Aβ40 fibril structures have been determined. The mechanism of why one particular protein sequence adopts so many different three-dimensional structures is yet not understood. In this work, we describe the assignment of the NMR chemical shifts of two Alzheimer's disease fibril polymorphs, P1 and P2, which are formed by the amyloid-beta peptide Aβ40. The assignment is based on 13C-detected 3D NCACX and NCOCX experiments MAS solid-state NMR experiments. The fibril samples are prepared using an extensive seeding protocol in the absence and presence of the small heat shock protein αB-crystallin. In addition to manual assignments, we obtain chemical shift assignments using the automation software ARTINA. We present an analysis of the secondary chemical shifts and a discussion on the differences between the manual and automated assignment strategies.
AU  - Rodina, N.
AU  - Sarkar, R.
AU  - Tsakalos, D.*
AU  - Suladze, S.*
AU  - Niu, Z.*
AU  - Reif, B.
C1  - 71444
C2  - 56177
CY  - Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands
TI  - Manual and automatic assignment of two different Aβ40 amyloid fibril polymorphs using MAS solid-state NMR spectroscopy.
JO  - Biomol. NMR Assign.
PB  - Springer
PY  - 2024
SN  - 1874-2718
ER  - 

TY  - JOUR
AB  - The aggregation of antibody light chains is linked to systemic light chain (AL) amyloidosis, a disease where amyloid deposits frequently affect the heart and the kidney. We here investigate fibrils from the lambda-III FOR005 light chain (LC), which is derived from an AL-patient with severe cardiac involvement. In FOR005, five residues are mutated with respect to its closest germline gene segment IGLV3-19 and IGLJ3. All mutations are located close to the complementarity determining regions (CDRs). The sequence segments responsible for the fibril formation are not yet known. We use fibrils extracted from the heart of this particular amyloidosis patient as seeds to prepare fibrils for solid-state NMR. We show that the seeds induce the formation of a specific fibril structure from the biochemically produced protein. We have assigned the fibril core region of the FOR005-derived fibrils and characterized the secondary structure propensity of the observed amino acids. As the primary structure of the aggregated patient protein is different for every AL patient, it is important to study, analyze and report a greater number of light chain sequences associated with AL amyloidosis.
AU  - Pradhan, T.
AU  - Annamalai, K.*
AU  - Sarkar, R.
AU  - Hegenbart, U.*
AU  - Schönland, S.*
AU  - Fändrich, M.*
AU  - Reif, B.
C1  - 60078
C2  - 49224
CY  - Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands
SP  - 9-16
TI  - Solid state NMR assignments of a human λ-III immunoglobulin light chain amyloid fibril.
JO  - Biomol. NMR Assign.
VL  - 15
IS  - 1
PB  - Springer
PY  - 2021
SN  - 1874-2718
ER  - 

TY  - JOUR
AB  - G-proteins are essential switch points at the cell membrane that control downstream signaling by their ability to adopt an inactive, GDP-bound or an active, GTP-bound state. Among other exchange factors, G-protein coupled receptors (GPCRs) induce exchange of GDP to GTP and thus promote the active state of the G-protein. The nucleotide-binding subunit of the G-protein undergoes major conformational changes upon nucleotide binding. Thus, an NMR analysis of the two distinct nucleotide-bound states is essential for a more detailed understanding of associated structural changes. Here, we provide an NMR backbone as well as methyl group resonance assignment of an inhibitory G-alpha subunit subtype 1 (G(i,1)) in the GDP-bound form and show that, in contrast to the GTP-bound form, large parts of the protein are mobile, presumably caused by a loose arrangement of the two subdomains in G that tightly interact with each other only in the GTP-bound state. As the GDP-bound form represents the GPCR-binding-competent state, the presented NMR data will be essential for further studies on G-protein-GPCR interactions and dynamics in solution for receptor systems that couple to G-proteins containing an inhibitory G,1 subunit.
AU  - Goricanec, D.
AU  - Hagn, F.
C1  - 54959
C2  - 45985
CY  - Van Godewijckstraat 30, 3311 Gz Dordrecht, Netherlands
SP  - 131-137
TI  - NMR backbone and methyl resonance assignments of an inhibitory G-alpha subunit in complex with GDP.
JO  - Biomol. NMR Assign.
VL  - 13
IS  - 1
PB  - Springer
PY  - 2019
SN  - 1874-2718
ER  - 

TY  - JOUR
AB  - FAT C-terminal (FATC) is a circa 33 residue-long domain. It controls the kinase functionality in phosphatidylinositol-3 kinase-related kinases (PIKKs). Recent NMR- and CD-monitored interaction studies indicated that the FATC domains of all PIKKs can interact with membrane mimetics albeit with different preferences for membrane properties such as surface charge and curvature. Thus they may generally act as membrane anchoring unit. Here, we present the H-1, N-15, and C-13 chemical shift assignments of the DPC micelle immersed FATC domains of the human PIKKs ataxia-telangiectasia mutated (ATM, residues 3024-3056) and DNA protein kinase catalytic subunit (DNA-PKcs, residues 4096-4128), both fused to the 56 residue long B1 domain of Streptococcal protein G (GB1). Each fusion protein is 100 amino acids long and contains in the linking region between the GB1 tag and the FATC region a thrombin (LVPRGS) and an enterokinase (DDDDK) protease site. The assignments pave the route for the detailed structural characterization of the membrane mimetic bound states, which will help to better understand the role of the proper cellular localization at membranes for the function and regulation of PIKKs. The chemical shift assignment of the GB1 tag is useful for NMR spectroscopists developing new experiments or using GB1 otherwise for case studies in the field of in-cell NMR spectroscopy or protein folding. Moreover it is often used as purification tag. Earlier we showed already that GB1 does not interact with membrane mimetics and thus does not disturb the NMR monitoring of membrane mimetic interactions of attached proteins.
AU  - Rahim, M.S.A.*
AU  - Sommer, L.A.M.*
AU  - Wacker, A.*
AU  - Schaad, M.*
AU  - Dames, S.A.
C1  - 52800
C2  - 44449
CY  - Dordrecht
SP  - 149-154
TI  - H-1, N-15, and C-13 chemical shift assignments of the micelle immersed FAT C-terminal (FATC) domains of the human protein kinases ataxia-telangiectasia mutated (ATM) and DNA-dependent protein kinase catalytic subunit (DNA-PKcs) fused to the B1 domain of streptococcal protein G (GB1).
JO  - Biomol. NMR Assign.
VL  - 12
IS  - 1
PB  - Springer
PY  - 2018
SN  - 1874-2718
ER  - 

TY  - JOUR
AB  - Mycobacterium tuberculosis protein kinase G (PknG) is a 82 kDa multidomain eukaryotic-like serine/threonine kinase mediating the survival of pathogenic mycobacteria within host macrophages. The N-terminal sequence preceding the catalytic kinase domain contains an approximately 75 residues long tail, which was predicted to show no regulatory secondary structure (1–75 = NORS) but harbors the major in vivo phosphorylation site (T63), and a rubredoxin-like metal binding motif (74–147 = RD). In the reduced rubredoxin motif, four conserved cysteine residues that are present as two C-X-X-C-G motifs coordinate a metal ion. The cysteines are further involved in sensing the redox environment to regulate PknG catalytic activity. Here, we report the 1H, 13C, and 15N resonance assignments of the highly dynamic unstructured N-terminal region NORS and the RD in the reduced, metal bound, presumably folded and the oxidized, presumably unfolded state. Chemical shifts have been deposited at the BioMagResBank under the BMRB accession numbers 26,028 for the His-PknG1–147 with the RD in reduced, metal bound state, 26,027 for His-PknG1–75, and 26,030 and 26,029 for PknG74–147 either in the reduced, metal bound or oxidized state, respectively. The presented chemical shift assignments pave the route for the structural characterization of the regulation of PknG by redox changes and posttranslational modifications (phosphorylation).
AU  - Wittwer, M.*
AU  - Dames, S.A.
C1  - 49514
C2  - 30633
CY  - Dordrecht
SP  - 401-406
TI  - Chemical shift assignment of the intrinsically disordered N-terminus and the rubredoxin domain in the folded metal bound and unfolded oxidized state of mycobacterial protein kinase G.
JO  - Biomol. NMR Assign.
VL  - 10
IS  - 2
PB  - Springer
PY  - 2016
SN  - 1874-2718
ER  - 

TY  - JOUR
AB  - Initiation of X-chromosome inactivation in female mammals depends on the non-coding RNA Xist. We have solved the NMR structure of a 14-nucleotide hairpin with a novel AUCG tetraloop fold from a Xist A-repeat that is essential for silencing. The (1)H, (13)C, (15)N and (31)P chemical shift assignments are reported.
AU  - Duszczyk, M.M.
AU  - Sattler, M.
C1  - 6628
C2  - 29007
CY  - Dordrecht, Netherlands
SP  - 75-77
TI  - 1H, 13C, 15N and 31P chemical shift assignments of a human Xist RNA A-repeat tetraloop hairpin essential for X-chromosome inactivation.
JO  - Biomol. NMR Assign.
VL  - 6
IS  - 1
PB  - Springer
PY  - 2012
SN  - 1874-2718
ER  - 

TY  - JOUR
AB  - The interleukin-4-inducing principle from Schistosoma mansoni eggs (IPSE/alpha-1) is a major immunogenic component of schistosomes. It potently triggers the release of interleukin-4 from basophilic granulocytes in an IgE-dependent manner, suggesting a key function in the modulation of the host's immune response to Schistosoma mansoni infection. Here we present the near complete assignment of an IPSE/alpha-1 variant, IPSEΔNLS, which comprises the core domain of the protein.
AU  - Meyer, N.H.
AU  - Schramm, G.*
AU  - Sattler, M.
C1  - 6632
C2  - 29011
CY  - Dordrecht, Netherlands
SP  - 225-227
TI  - 1H, 13C and 15N chemical shift assignments of IPSEΔNLS.
JO  - Biomol. NMR Assign.
VL  - 5
IS  - 2
PB  - Springer
PY  - 2011
SN  - 1874-2718
ER  - 

TY  - JOUR
AB  - U2AF homology motifs (UHM) are protein domains that bind peptidic UHM ligand motifs (ULM) and thus form an intricate network of interactions involved in splicing regulation. Here, we report the backbone assignment of the UHM domain of the splicing factor Puf60 as well as H-1, N-15 chemical shifts upon binding of the ULM peptides U2AF(65) (85-112), SF1 (1-25), SF3b155 (194-229), SF3b155 (317-357), and Prp16 (201-238).
AU  - Corsini, L.*
AU  - Sattler, M.
C1  - 404
C2  - 25938
SP  - 211-214
TI  - Backbone assignment of the UHM domain of Puf60 free and bound to five ligands.
JO  - Biomol. NMR Assign.
VL  - 2
IS  - 2
PB  - Springer
PY  - 2008
SN  - 1874-2718
ER  - 

TY  - JOUR
AB  - EH domains are protein-protein interaction domains that function in vesicular trafficking and endocytosis. Here, we report the NMR spectral assignments of the high-affinity complex between the second EH domain of Eps15 and a stonin 2 peptide-providing the basis for the characterization of a two-site binding mode.
AU  - Rumpf, J.*
AU  - Simon, B.*
AU  - Groemping, Y.*
AU  - Sattler, M.
C1  - 1756
C2  - 25936
SP  - 55-58
TI  - H-1, C-13, and N-15 chemical shift assignments for the Eps15-EH2-stonin 2 complex.
JO  - Biomol. NMR Assign.
VL  - 2
IS  - 1
PB  - Springer
PY  - 2008
SN  - 1874-2718
ER  -