Syndecan-4 (SDC4) consists of transmembrane heparan sulfate proteoglycan (HSPG) belonging to the syndecan family. It is present in most cell types of Mammalia. Its structure contains a heparan-sulfate-modified extracellular domain, a single transmembrane domain, and a short C-terminal cytoplasmic domain. Regarding the overall cellular function of SDC4, other cells or ligands can bind to its ecto-domain. In addition, 4,5-bisphosphate phosphatidylinositol (PIP(2)) or protein kinase C? can bind to...
[NMR paper] Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes from (31)P NMR
Interactions of HIV gp41's membrane-proximal external region and transmembrane domain with phospholipid membranes from (31)P NMR
HIV-1 entry into cells requires coordinated changes of the conformation and dynamics of both the fusion protein, gp41, and the lipids in the cell membrane and virus envelope. Commonly proposed features of membrane deformation during fusion include high membrane curvature, lipid disorder, and membrane surface dehydration. The virus envelope and target cell membrane contain a diverse set of phospholipids and cholesterol. To dissect how different lipids interact...
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[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 Articles 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.
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
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AIIt, a...
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[NMR paper] Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles Toll-like receptor 3 transmembrane domain is able to perform various homotypic interactions: an NMR structural study.
FEBS Lett. 2014 Nov 3;588(21):3802-7
Authors: Mineev KS, Goncharuk SA, Arseniev AS
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Toll-like receptors (TLRs) take part in both the innate and...
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[NMR paper] Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy.
Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy.
Related Articles Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy.
Biochim Biophys Acta. 2013 Jun 14;
Authors: Choudhury AR, Perdih A, Zuperl S, Sikorska E, Solmajer T, Jurga S, Zhukov I, Novi? M
Abstract
Membrane proteins...
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Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy
Structural Elucidation of Transmembrane Transporter Protein Bilitranslocase: Conformational analysis of the second transmembrane region TM2 by molecular dynamics and NMR spectroscopy
Publication date: Available online 14 June 2013
Source:Biochimica et Biophysica Acta (BBA) - Biomembranes</br>
Author(s): Amrita Roy Choudhury , Andrej Perdih , Špela Župerl , Emilia Sikorska , Tom Solmajer , Stefan Jurga , Igor Zhukov , Marjana Novi?</br>
Membrane proteins represent about a third of the gene products in most organisms, as revealed by the genome sequencing...
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[NMR paper] Investigating the conformational coupling between the transmembrane and cytoplasmic d
Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
Related Articles Investigating the conformational coupling between the transmembrane and cytoplasmic domains of a single-spanning membrane protein. A 1H-NMR study.
FEBS Lett. 2001 Sep 21;505(3):431-5
Authors: Mousson F, Beswick V, Coïc YM, Huynh-Dinh T, Sanson A, Neumann JM
PMP1 is a 38-residue single-spanning membrane protein whose C-terminal cytoplasmic domain, Y25-F38, is highly positively...
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[NMR paper] Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bil
Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bilayers.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--pubs.acs.org-images-acspubs.jpg Related Articles Oligomerization of the EGF receptor transmembrane domain: a 2H NMR study in lipid bilayers.
Biochemistry. 1997 Oct 14;36(41):12616-24
Authors: Jones DH, Rigby AC, Barber KR, Grant CW
During the course of a previous study by wideline 2H NMR, we noted spectral features suggesting the possibility of monitoring homodimer/oligomer interactions between...
NMR Structural Study of Syndecan-4 Transmembrane Domain with Cytoplasmic Region
Linear Mode
