Solution NMR reveals the structure and dynamics of biomolecules in solution. In particular, the method can detect changes due to perturbation of the molecules, without limiting effects of frozen particles or crystal environments. Phytochromes are photosensors which control the response to red/far-red light in bacteria, fungi and plants, undergo specific structural changes when photoactivated from the Pr to the Pfr state. While structures of phytochromes have been revealed in both states, the...
[NMR paper] Solution NMR backbone resonance assignment of the full-length resistance-related calcium-binding protein Sorcin
Solution NMR backbone resonance assignment of the full-length resistance-related calcium-binding protein Sorcin
Sorcin is a penta-EF hand calcium-binding protein that confers multidrug resistance in cancer cells. It regulates cellular Ca^(2+) homeostasis by interacting with calcium channels such as Ryanodine receptor 2 and Sarcoplasmic/endoplasmic reticulum Ca^(2+)-ATPase in a calcium-dependent manner. The crystal structure of the Sorcin has been determined in both calcium-free and calcium-bound states to understand calcium-binding induced conformational change. However, due to its...
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09-02-2024 02:54 AM
[NMR paper] Solution NMR backbone assignment of the SASH1 SLy proteins associated disordered region (SPIDER)
Solution NMR backbone assignment of the SASH1 SLy proteins associated disordered region (SPIDER)
SASH1 is a scaffold protein with context-dependent biological functions in cell adhesion, tumor metastasis, lung development, and pigmentation. As a member of the SLy protein family, it contains the conserved SLY, SH3, and SAM domains. The 19 kDa SLY domain harbors over 70% of the SASH1 variants associated with pigmentation disorders. However, its solution structure or dynamics have not been investigated yet, and its exact position in the sequence is not clearly defined. Based on the...
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05-10-2023 09:54 AM
[NMR paper] 1H, 13C, 15N backbone resonance assignment of apo and ADP-ribose bound forms of the macro domain of Hepatitis E virus through solution NMR spectroscopy
1H, 13C, 15N backbone resonance assignment of apo and ADP-ribose bound forms of the macro domain of Hepatitis E virus through solution NMR spectroscopy
The genome of Hepatitis E virus (HEV) is 7.2 kilobases long and has three open reading frames. The largest one is ORF1, encoding a non-structural protein involved in the replication process, and whose processing is ill-defined. The ORF1 protein is a multi-modular protein which includes a macro domain (MD). MDs are evolutionarily conserved structures throughout all kingdoms of life. MDs participate in the recognition and removal of...
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10-23-2022 06:26 PM
[NMR paper] Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR.
Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR.
Related Articles Co-refolding of a functional complex of Dengue NS3 protease and NS2B co-factor domain and backbone resonance assignment by solution NMR.
Protein Expr Purif. 2017 Jul 24;:
Authors: Woestenenk E, Agback P, Unnerståle S, Henderson I, Agback T
Abstract
A novel approach for separate expression of dengue virus NS3 protease and its NS2B cofactor domain is described in this paper. The...
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07-29-2017 10:35 AM
[NMR paper] NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
NMR backbone resonance assignment and solution secondary structure determination of human NSD1 and NSD2.
Biomol NMR Assign. 2016 Jun 29;
Authors: Amin N, Nietlispach D, Qamar S, Coyle J, Chiarparin E, Williams G
Abstract
Proteins of the NSD family are histone-methyl transferases with critical functions in the regulation of chromatin structure and function. NSD1 and NSD2 are homologous proteins that function as epigenetic...
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07-01-2016 03:22 PM
[NMR paper] Backbone Assignment of the MALT1 Paracaspase by Solution NMR.
Backbone Assignment of the MALT1 Paracaspase by Solution NMR.
Backbone Assignment of the MALT1 Paracaspase by Solution NMR.
PLoS One. 2016;11(1):e0146496
Authors: Unnerståle S, Nowakowski M, Baraznenok V, Stenberg G, Lindberg J, Mayzel M, Orekhov V, Agback T
Abstract
Mucosa-associated lymphoid tissue lymphoma translocation protein 1 (MALT1) is a unique paracaspase protein whose protease activity mediates oncogenic NF-?B signalling in activated B cell-like diffuse large B cell lymphomas (ABC-DLBCLs). ABC-DLBCLs are aggressive...
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01-21-2016 01:08 PM
[NMR paper] NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans.
NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of the N-terminal-most HRDC1 domain of RecQ helicase from Deinococcus radiodurans.
FEBS Lett. 2013 Aug 19;587(16):2635-42
Authors: Liu S, Zhang W, Gao Z, Ming Q, Hou H, Lan W, Wu H, Cao C, Dong Y
Abstract
The RecQ helicase from Deinococcus radiodurans (DrRecQ) distinguishes from other...
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10-24-2013 08:45 PM
Expression, Purification, Detergent Screening and Solution NMR Backbone Assignment of
Expression, Purification, Detergent Screening and Solution NMR Backbone Assignment of the Human Potassium Channel Accessory Subunit MiRP1.
Expression, Purification, Detergent Screening and Solution NMR Backbone Assignment of the Human Potassium Channel Accessory Subunit MiRP1.
Protein Expr Purif. 2010 Nov 15;
Authors: Chen L, Lai C, Lai J, Tian C
MiRP1 (MinK related protein 1) is a membrane protein in the KCNE family. It can associate with and modulate various voltage gated potassium channels. Mutations in human MiRP1 have been found to cause many...