[NMR paper] Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Related ArticlesAssigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Biomol NMR Assign. 2020 Apr 20;:
Authors: Schulte T, Sala BM, Nilvebrant J, Nygren PÅ, Achour A, Shernyukov A, Agback T, Agback P
Abstract
The pneumococcal serine rich repeat protein (PsrP) is displayed on the surface of Streptococcus pneumoniae with a suggested role in colonization in the human upper respiratory tract. Full-length PsrP is a 4000 residue-long multi-domain protein comprising a positively charged functional binding region (BR) domain for interaction with keratin and extracellular DNA during pneumococcal adhesion and biofilm formation, respectively. The previously determined crystal structure of the BR domain revealed a flat compressed barrel comprising two sides with an extended ?-sheet on one side, and another ?-sheet that is distorted by loops and ?-turns on the other side. Crystallographic B-factors indicated a relatively high mobility of loop regions that were hypothesized to be important for binding. Furthermore, the crystal structure revealed an inter-molecular ?-sheet formed between edge strands of two symmetry-related molecules, which could promote bacterial aggregation during biofilm formation. Here we report the near complete 15N/13C/1H backbone resonance assignment of the BR domain of PsrP, revealing a secondary structure profile that is almost identical to the X-ray structure. Dynamic 15N-T1, T2 and NOE data suggest a monomeric and rigid structure of BR with disordered residues only at the N- and C-termini. The presented peak assignment will allow us to identify BR residues that are crucial for ligand binding.
PMID: 32314099 [PubMed - as supplied by publisher]
[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...
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03-17-2018 12:12 PM
A Noncanonical Binding Site in the EVH1 Domain ofVasodilator-Stimulated Phosphoprotein Regulates Its Interactions withthe Proline Rich Region of Zyxin
A Noncanonical Binding Site in the EVH1 Domain ofVasodilator-Stimulated Phosphoprotein Regulates Its Interactions withthe Proline Rich Region of Zyxin
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/bichaw/0/bichaw.ahead-of-print/acs.biochem.7b00618/20170823/images/medium/bi-2017-006182_0008.gif
Biochemistry
DOI: 10.1021/acs.biochem.7b00618
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08-24-2017 08:38 AM
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Abstract
Chemokine CXCL8 and its receptor CXCR1 are key mediators in combating infection and have also been implicated in the pathophysiology of various diseases including chronic obstructive pulmonary disease (COPD) and cancer. CXCL8 exists as monomers and dimers but monomer alone binds CXCR1 with high affinity. CXCL8 function involves binding two distinct CXCR1 sites – the N-terminal domain (Site-I) and the extracellular/transmembrane domain (Site-II). Therefore, higher monomer affinity...
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[NMR paper] Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--media.wiley.com-assets-2250-98-WileyOnlineLibrary-Button_120x27px_FullText.gif Related Articles Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain.
Protein Sci. 2014 Oct 18;
Authors: Joseph PR, Rajarathnam K
Abstract
Chemokine CXCL8 and its receptor CXCR1 are key mediators in combating infection and have also been...
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10-21-2014 11:31 PM
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Solution NMR characterization of WT CXCL8 monomer and dimer binding to CXCR1 N-terminal domain
Abstract
Chemokine CXCL8 and its receptor CXCR1 are key mediators in combating infection and have also been implicated in the pathophysiology of various diseases including chronic obstructive pulmonary disease (COPD) and cancer. CXCL8 exists as monomers and dimers but monomer alone binds CXCR1 with high affinity. CXCL8 function involves binding two distinct CXCR1 sites – the N-terminal domain (Site-I) and the extracellular/transmembrane domain (Site-II). Therefore, higher monomer affinity...
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10-18-2014 09:26 PM
[NMR paper] NMR assignment of the R2 domain of pneumococcal choline binding protein A (CbpA).
NMR assignment of the R2 domain of pneumococcal choline binding protein A (CbpA).
Related Articles NMR assignment of the R2 domain of pneumococcal choline binding protein A (CbpA).
J Biomol NMR. 2005 May;32(1):93
Authors: Luo R, Mann B, Tuomanen E, Kriwacki RW
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[NMR paper] NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli Dna
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
J Mol Biol. 1996 Jul 12;260(2):236-50
Authors: Pellecchia M, Szyperski T, Wall D, Georgopoulos C, Wüthrich K
The recombinant N-terminal 107-amino acid polypeptide fragment 2-108 of the DnaJ molecular chaperone of Escherichia...
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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...
Assigned NMR backbone resonances of the ligand-binding region domain of the pneumococcal serine-rich repeat protein (PsrP-BR) reveal a rigid monomer in solution.
Linear Mode
