[NMR paper] Structural characterization of a dimeric complex between the short cytoplasmic domain of CEACAM1 and the pseudo tetramer of S100A10-Annexin A2 using NMR and molecular dynamics.
Structural characterization of a dimeric complex between the short cytoplasmic domain of CEACAM1 and the pseudo tetramer of S100A10-Annexin A2 using NMR and molecular dynamics.
Related ArticlesStructural characterization of a dimeric complex between the short cytoplasmic domain of CEACAM1 and the pseudo tetramer of S100A10-Annexin A2 using NMR and molecular dynamics.
Biochim Biophys Acta Biomembr. 2020 Aug 21;:183451
Authors: Hu W, Bhattacharya S, Hong T, Wong P, Li L, Vaidehi N, Kalkum M, Shively JE
Abstract
AIIt, a heterotetramer of S100A10 (P11) and Annexin A2, plays a key role in calcium dependent, membrane associations with a variety of proteins. We previously showed that AIIt interacts with the short cytoplasmic domain (12 amino acids) of CEACAM1 (CEACAM1-SF). Since the cytoplasmic domains of CEACAM1 help regulate the formation of cis- or trans-dimers at the cell membrane, we investigated the possible role of their association with AIIt in this process. Using NMR and molecular dynamics, we show that AIIt and its pseudoheterodimer interacts with two molecules of short cytoplasmic domain isoform peptides, and that interaction depends on the binding motif 454-Phe-Gly-Lys-Thr-457 where Phe-454 binds in a hydrophobic pocket of AIIt, the null mutation Phe454Ala reduces binding by 2.5 fold, and the pseudophosphorylation mutant Thr457Glu reduces binding by three fold. Since these two residues in CEACAM1-SF were also found to play a role in the binding of calmodulin and G-actin at the membrane, we hypothesize a sequential set of three interactions are responsible for regulation of cis- to trans-dimerization of CEACAM1. The hydrophobic binding pocket in AIIt corresponds to a previously identified binding pocket for a peptide found in SMARCA3 and AHNAK, suggesting a conserved functional motif in AIIt allowing multiple proteins to reversibly interact with integral membrane proteins in a calcium dependent manner.
PMID: 32835655 [PubMed - as supplied by publisher]
[NMR paper] NMR Structure, Dynamics and Interactions of the Integrin ?2 Cytoplasmic Tail with Filamin Domain IgFLNa21.
NMR Structure, Dynamics and Interactions of the Integrin ?2 Cytoplasmic Tail with Filamin Domain IgFLNa21.
Related Articles NMR Structure, Dynamics and Interactions of the Integrin ?2 Cytoplasmic Tail with Filamin Domain IgFLNa21.
Sci Rep. 2018 Apr 03;8(1):5490
Authors: Chatterjee D, Zhiping LL, Tan SM, Bhattacharjya S
Abstract
Integrins are transmembrane proteins that mediate cell adhesion and migration. Each integrin is a heterodimer formed by an ? and a ? subunit. A large number of cytoplasmic proteins interact with the...
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[NMR paper] Combined molecular dynamics, STD-NMR, and CORCEMA protocol yields structural model for a UDP-galactopyranose mutase-inhibitor complex.
Combined molecular dynamics, STD-NMR, and CORCEMA protocol yields structural model for a UDP-galactopyranose mutase-inhibitor complex.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Combined molecular dynamics, STD-NMR, and CORCEMA protocol yields structural model for a UDP-galactopyranose mutase-inhibitor complex.
Bioorg Med Chem Lett. 2015 Mar 15;25(6):1284-7
Authors: Shi Y, Ardá A, Pinto BM
Abstract
UDP-galactopyranose mutase (UGM) is...
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Chemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domain
Chemical ligation of the influenza M2 protein for solid-state NMR characterization of the cytoplasmic domain
Abstract
Solid-state NMR-based structure determination of membrane proteins and large protein complexes faces the challenge of limited spectral resolution when the proteins are uniformly 13C-labeled. A strategy to meet this challenge is chemical ligation combined with site-specific or segmental labeling. While chemical ligation has been adopted in NMR studies of water-soluble proteins, it has not been demonstrated for membrane proteins. Here we show chemical ligation of the...
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[NMR paper] Chemical Ligation of the Influenza M2 Protein for Solid-State NMR Characterization of the Cytoplasmic Domain.
Chemical Ligation of the Influenza M2 Protein for Solid-State NMR Characterization of the Cytoplasmic Domain.
Related Articles Chemical Ligation of the Influenza M2 Protein for Solid-State NMR Characterization of the Cytoplasmic Domain.
Protein Sci. 2015 May 13;
Authors: Kwon B, Tietze D, White PB, Liao SY, Hong M
Abstract
Solid-state NMR-based structure determination of membrane proteins and large protein complexes faces the challenge of limited spectral resolution when the proteins are uniformly (13) C-labeled. A strategy to...
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05-15-2015 08:02 PM
Chemical Ligation of the Influenza M2 Protein for Solid-State NMR Characterization of the Cytoplasmic Domain
Chemical Ligation of the Influenza M2 Protein for Solid-State NMR Characterization of the Cytoplasmic Domain
Abstract
Solid-state NMR-based structure determination of membrane proteins and large protein complexes faces the challenge of limited spectral resolution when the proteins are uniformly 13C-labeled. A strategy to meet this challenge is chemical ligation combined with site-specific or segmental labeling. While chemical ligation has been adopted in NMR studies of water-soluble proteins, it has not been demonstrated for membrane proteins. Here we show chemical ligation of the...
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05-13-2015 02:01 PM
[NMR paper] pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study.
pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-pubmed-acspubs.jpg Related Articles pH-Independence of trialanine and the effects of termini blocking in short peptides: a combined vibrational, NMR, UVCD, and molecular dynamics study.
J Phys Chem B. 2013 Apr 11;117(14):3689-706
Authors: Toal S, Meral D, Verbaro D, Urbanc B, Schweitzer-Stenner R
Abstract...
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Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Structural characterization of recombinant human myoglobin isoforms by (1)H and (129)Xe NMR and molecular dynamics simulations.
Biochim Biophys Acta. 2011 Jul 13;
Authors: Gussoni M, Scorciapino MA, Vezzoli A, Anedda R, Greco F, Ceccarelli M, Casu M
Myoglobin (Mb), the main cytosolic oxygen storage/deliver protein, is also known to interact with different small ligands exerting other fundamental physiological roles. In...
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[NMR paper] Folding properties of an annexin I domain: a 1H-15N NMR and CD study.
Folding properties of an annexin I domain: a 1H-15N NMR and CD study.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Folding properties of an annexin I domain: a 1H-15N NMR and CD study.
Biochemistry. 1996 Aug 13;35(32):10347-57
Authors: Cordier-Ochsenbein F, Guerois R, Baleux F, Huynh-Dinh T, Chaffotte A, Neumann JM, Sanson A
The annexin fold consists of four 70-residue domains with markedly homologous sequences and nearly identical structures. Each domain contains five helices...
Structural characterization of a dimeric complex between the short cytoplasmic domain of CEACAM1 and the pseudo tetramer of S100A10-Annexin A2 using NMR and molecular dynamics.
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