Related ArticlesNMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.
Comput Struct Biotechnol J. 2014;9:e201402003
Authors: Barbar E, Nyarko A
Abstract
Most proteins in interaction networks have a small number of partners, while a few, called hubs, participate in a large number of interactions and play a central role in cell homeostasis. One highly conserved hub is a protein called LC8 that was originally identified as an essential component of the multi-subunit complex dynein but later shown to be also critical in multiple protein complexes in diverse systems. What is intriguing about this hub protein is that it does not passively bind its various partners but emerging evidence suggests that LC8 acts as a dimerization engine that promotes self-association and/or higher order organization of its primarily disordered monomeric partners. This structural organization process does not require ATP but is triggered by long-range allosteric regulation initiated by LC8 binding a pair of disordered chains forming a bivalent or polybivalent scaffold. This review focuses on the role of LC8 in promoting self-association of two of its binding partners, a dynein intermediate chain and a non dynein protein called Swallow.
PMID: 24757501 [PubMed - as supplied by publisher]
[NMR paper] Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Characterization of residue-dependent differences in the peripheral membrane association of the FATC domain of the kinase 'target of rapamycin' by NMR and CD spectroscopy.
FEBS Lett. 2014 Apr 3;
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NMR investigations of metal interactions with unstructured soluble protein domains
NMR investigations of metal interactions with unstructured soluble protein domains
Publication date: Available online 28 February 2014
Source:Coordination Chemistry Reviews</br>
Author(s): Riccardo De Ricco , Slawomir Potocki , Henryk Kozlowski , Daniela Valensin</br>
Essential main-group elements and transition metal ions play key roles in the structural organization and biological function of many macromolecules such as proteins, DNA, and RNA. Healthy conditions require tight regulation of metal concentrations inside and outside cells, and both metal...
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NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
NMR Characterization of Copper-Binding Domains 4-6 of ATP7B,
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Biochemistry
DOI: 10.1021/bi1008535
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NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Related Articles NMR Characterization of Copper-binding Domains 4-6 of ATP7B.
Biochemistry. 2010 Aug 27;
Authors: Fatemi N, Korzhnev DM, VÄ?lyvis A, Sarkar B, Forman-Kay JD
The Wilson disease protein (ATP7B) is a copper-transporting member of the P-type ATPase superfamily, which plays a central role in copper homeostasis and interacts with the copper chaperone Atox1. The N-terminus of ATP7B is comprised of six copper-binding domains (WCBDs), each capable of binding one copper atom in the...
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[NMR paper] NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the D
NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with target RNA fragments with site-specific uridine substitutions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with...
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[NMR paper] NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the D
NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with target RNA fragments with site-specific uridine substitutions.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-custom-oxfordjournals_final_free.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles NMR analysis of the hydrogen bonding interactions of the RNA-binding domains of the Drosophila sex-lethal protein with...
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[NMR paper] Characterization of tertiary interactions in a folded protein by NMR methods: studies
Characterization of tertiary interactions in a folded protein by NMR methods: studies of pH-induced structural changes in human growth hormone.
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Biochemistry. 1992 Sep 15;31(36):8587-96
Authors: Abildgaard F, Jørgensen AM, Led JJ, Christensen T, Jensen EB, Junker F, Dalbøge H
The pH-induced conformational changes in human growth hormone (hGH) have been studied, using a new...
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NMR characterization of foldedness for the production of E3 RING domains.
NMR characterization of foldedness for the production of E3 RING domains.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR characterization of foldedness for the production of E3 RING domains.
J Struct Biol. 2010 Aug 2;
Authors: Huang A, de Jong RN, Folkers GE, Boelens R
We summarize the use of NMR spectroscopy in the production and the screening of stability and foldedness of protein domains, and apply it to the RING domains of E3 ubiquitin-ligases. RING domains...
NMR Characterization of Self-Association Domains Promoted by Interactions with LC8 Hub Protein.
Linear Mode
