Related ArticlesNMR Characterization and Membrane Interactions of the Loop Region of Kindlin-3 F1 Subdomain.
PLoS One. 2016;11(4):e0153501
Authors: Chua GL, Tan SM, Bhattacharjya S
Abstract
Kindlins-1,2 and 3 are FERM domain-containing cytosolic proteins involved in the activation and regulation of integrin-mediated cell adhesion. Apart from binding to integrin ? cytosolic tails, kindlins and the well characterized integrin-activator talin bind membrane phospholipids. The ubiquitin-like F1 sub-domain of the FERM domain of talin contains a short loop that binds to the lipid membrane. By contrast, the F1 sub-domain of kindlins contains a long loop demonstrated binding to the membrane. Here, we report structural characterization and lipid interactions of the 83-residue F1 loop of kindlin-3 using NMR and optical spectroscopy methods. NMR studies demonstrated that the F1 loop of kindlin-3 is globally unfolded but stretches of residues assuming transient helical conformations could be detected in aqueous solution. We mapped membrane binding interactions of the F1 loop with small unilamellar vesicles (SUVs) containing either zwitterionic lipids or negatively charged lipids using 15N-1H HSQC titrations. These experiments revealed that the F1 loop of kindlin-3 preferentially interacted with the negatively charged SUVs employing almost all of the residues. By contrast, only fewer residues appeared to be interacted with SUVs containing neutral lipids. Further, CD and NMR data suggested stabilization of helical conformations and predominant resonance perturbations of the F1 loop in detergent containing solutions. Conformations of an isolated N-terminal peptide fragment, or EK21, of the F1 loop, containing a poly-Lys sequence motif, important for membrane interactions, were also investigated in detergent solutions. EK21 adopted a rather extended or ?-type conformations in complex with negatively charged SDS micelles. To our knowledge, this is the first report describing the conformations and residue-specific interactions of kindlin F1 loop with lipids. These data therefore provide important insights into the interactions of kindlin FERM domain with membrane lipids that contribute toward the integrin activating property.
PMID: 27101375 [PubMed - as supplied by publisher]
Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions
Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions
Abstract
The membrane proteins of viruses play critical roles in the virus life cycle and are attractive targets for therapeutic intervention. Virus-like particles (VLP) present the possibility to study the biochemical and biophysical properties of viral membrane proteins in their native environment. Specifically, the VLP constructs contain the entire protein sequence and are comprised of native membrane components including lipids, cholesterol,...
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[NMR paper] Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions.
Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions.
Application of virus-like particles (VLP) to NMR characterization of viral membrane protein interactions.
J Biomol NMR. 2016 Feb 26;
Authors: Antanasijevic A, Kingsley C, Basu A, Bowlin TL, Rong L, Caffrey M
Abstract
The membrane proteins of viruses play critical roles in the virus life cycle and are attractive targets for therapeutic intervention. Virus-like particles (VLP) present the possibility to study the biochemical...
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[NMR paper] Solution NMR characterization of apical membrane antigen 1 and small molecule interactions as a basis for designing new antimalarials.
Solution NMR characterization of apical membrane antigen 1 and small molecule interactions as a basis for designing new antimalarials.
Related Articles Solution NMR characterization of apical membrane antigen 1 and small molecule interactions as a basis for designing new antimalarials.
J Mol Recognit. 2016 Jan 24;
Authors: Krishnarjuna B, Lim SS, Devine SM, Debono CO, Lam R, Chandrashekaran IR, Jaipuria G, Yagi H, Atreya HS, Scanlon MJ, MacRaild CA, Scammells PJ, Norton RS
Abstract
Plasmodium falciparum apical membrane antigen 1...
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Expression, purification and NMR characterization of the cyclic recombinant form of the third intracellular loop of the vasopressin type 2 receptor.
Expression, purification and NMR characterization of the cyclic recombinant form of the third intracellular loop of the vasopressin type 2 receptor.
Expression, purification and NMR characterization of the cyclic recombinant form of the third intracellular loop of the vasopressin type 2 receptor.
Protein Expr Purif. 2011 May 13;
Authors: Bellot G, Pascal R, Mendre C, Urbach S, Mouillac B, Déméné H
The vasopressin type 2 (V2R) receptor belongs to the class of G-protein coupled receptors. It is mainly expressed in the membrane of kidney tubules,...
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[NMR paper] Structural and dynamic characterization of the phosphotyrosine binding region of a Sr
Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches.
Related Articles Structural and dynamic characterization of the phosphotyrosine binding region of a Src homology 2 domain--phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches.
Biochemistry. 1995 Sep 12;34(36):11353-62
Authors: Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay JD
Arginine side chains are often...
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[NMR paper] Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region o
Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Structure of the metal-free gamma-carboxyglutamic acid-rich membrane binding region of factor IX by two-dimensional NMR spectroscopy.
J Biol Chem. 1995 Apr 7;270(14):7980-7
Authors: Freedman SJ, Furie BC, Furie B, Baleja JD
The gamma-carboxyglutamic acid-rich...
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[NMR paper] A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escheric
A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www3.interscience.wiley.com-aboutus-images-wiley_interscience_pubmed_logo_FREE_120x27.gif http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--www.pubmedcentral.nih.gov-corehtml-pmc-pmcgifs-pubmed-pmc.gif Related Articles A 19F-NMR study of the membrane-binding region of D-lactate dehydrogenase of Escherichia coli.
Protein Sci. 1993 Nov;2(11):1938-47
Authors: Sun ZY, Truong HT, Pratt EA, Sutherland DC,...
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[NMR paper] The mobile loop region of the NAD(H) binding component (dI) of proton-translocating n
The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles The mobile loop region of the NAD(H) binding component (dI) of proton-translocating nicotinamide nucleotide transhydrogenase from Rhodospirillum rubrum: complete NMR assignment and effects of bound nucleotides.
Biochim Biophys Acta. 1999...