Related ArticlesSolution NMR Determination of the CDHR3 Rhinovirus-C Binding Domain, EC1.
Viruses. 2021 Jan 22;13(2):
Authors: Lee W, Frederick RO, Tonelli M, Palmenberg AC
Abstract
Cadherin Related Family Member 3 (CDHR3) is the identified and required cellular receptor for all virus isolates in the rhinovirus-C species (RV-C). Cryo-EM determinations recently resolved the atomic structure of RV-C15a, and subsequently, a complex of this virus bound to CDHR3 extracellular domain 1 (EC1), the N-terminal portion of this receptor responsible for virus interactions. The EC1 binds to a hypervariable sequence footprint on the virus surface, near the 3-fold axis of icosahedral symmetry. The key contacts involve discontinuous residues from 3 viral proteins, VP1, VP2 and VP3. That single cryo-EM EC1 structure, however, could not resolve whether the virus-receptor interface was structurally adaptable to accommodate multiple virus sequences. We now report the solution NMR determination of CDHR3 EC1, showing that this protein, in fact, is mostly inflexible, particularly in the virus-binding face. The new, higher resolution dataset identifies 3 cis-Pro residues in important loop regions, where they can influence both rigidity and overall protein conformation. The data also provide clarification about the residues involved in essential calcium ion binding, and a potential CDHR3 surface groove feature that may be involved in native protein interactions with cellular partners.
[NMR paper] Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding.
Solution NMR Structure of the SH3 Domain of Human Caskin1 Validates the Lack of a Typical Peptide Binding Groove and Supports a Role in Lipid Mediator Binding.
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Cells. 2021 Jan 16;10(1):
Authors: T?ke O, Koprivanacz K, Radnai L, Mer? B, Juhász T, Liliom K, Buday L
Abstract
SH3 domains constitute an important class of protein modules involved in a variety of...
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[NMR paper] Solution NMR Studies of the Ligand-Binding Domain of an Orphan Nuclear Receptor Reveals a Dynamic Helix in the Ligand-Binding Pocket.
Solution NMR Studies of the Ligand-Binding Domain of an Orphan Nuclear Receptor Reveals a Dynamic Helix in the Ligand-Binding Pocket.
Solution NMR Studies of the Ligand-Binding Domain of an Orphan Nuclear Receptor Reveals a Dynamic Helix in the Ligand-Binding Pocket.
Biochemistry. 2018 Mar 16;:
Authors: Daffern N, Chen Z, Zhang Y, Pick L, Radhakrishnan I
Abstract
The ligand-binding domains (LBD) of the NR5A subfamily of nuclear receptors activate transcription via ligand-dependent and ligand-independent mechanisms. The...
[NMR paper] Solution NMR Structure of the DNA-binding Domain from Scml2 (Sex Comb on Midleg-like 2).
Solution NMR Structure of the DNA-binding Domain from Scml2 (Sex Comb on Midleg-like 2).
Solution NMR Structure of the DNA-binding Domain from Scml2 (Sex Comb on Midleg-like 2).
J Biol Chem. 2014 Apr 10;
Authors: Bezsonova I
Abstract
Scml2 is a member of the Polycomb group of proteins involved in epigenetic gene silencing. Human Scml2 is a part of a multi-subunit protein complex, PRC1 (Polycomb Repressive Complex 1), which is responsible for maintenance of gene repression, prevention of chromatin remodeling, preservation of...
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[NMR paper] Solution NMR Structure and Histone Binding of the PHD Domain of Human MLL5.
Solution NMR Structure and Histone Binding of the PHD Domain of Human MLL5.
Related Articles Solution NMR Structure and Histone Binding of the PHD Domain of Human MLL5.
PLoS One. 2013;8(10):e77020
Authors: Lemak A, Yee A, Wu H, Yap D, Zeng H, Dombrovski L, Houliston S, Aparicio S, Arrowsmith CH
Abstract
Mixed Lineage Leukemia 5 (MLL5) is a histone methyltransferase that plays a key role in hematopoiesis, spermatogenesis and cell cycle progression. In addition to its catalytic domain, MLL5 contains a PHD finger domain, a protein module that...
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10-17-2013 04:57 PM
[NMR paper] NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein
NMR solution structure of a peptide from the mdm-2 binding domain of the p53 protein that is selectively cytotoxic to cancer cells.
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Biochemistry. 2004 Feb 24;43(7):1854-61
Authors: Rosal R, Pincus MR, Brandt-Rauf PW, Fine RL, Michl J, Wang H
We have recently found that a peptide from the mdm-2 binding domain of the p53 protein induced rapid membranolytic necrosis of a variety of different human...
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[NMR paper] Determination of the solution structure of a synthetic two-site calcium-binding homod
Determination of the solution structure of a synthetic two-site calcium-binding homodimeric protein domain by NMR spectroscopy.
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Biochemistry. 1992 Oct 13;31(40):9572-80
Authors: Shaw GS, Hodges RS, Sykes BD
The solution structure of a 34-residue synthetic calcium-binding peptide from site III of chicken troponin-C has been determined by 1H NMR spectroscopy. In solution and in the presence of calcium...
Solution NMR Determination of the CDHR3 Rhinovirus-C Binding Domain, EC1.
Linear Mode
