Related ArticlesValidation of the binding site structure of the cellular retinol-binding protein (CRBP) by ligand NMR chemical shift perturbations.
J Am Chem Soc. 2005 Apr 20;127(15):5310-1
Authors: Wang B, Merz KM
We have calculated proton chemical shift perturbations (CSPs) of retinol in the cellular retinol-binding protein (CRBP) through the use of a recently developed computational approach (Wang et al. J. Chem. Phys. 2004, 120, 11392-11400). Excellent agreement with experimental values was obtained for the X-ray structure, whereas the lack of a key hydrogen bond and the distorted isoprene tail of retinol for some NMR models lead to large CSP RMSDs. Therefore, a comparison of computed CSPs of retinol with experiment offers a convenient way to validate the structure of retinol and its orientation in the binding site for the NMR structures.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Site-specific free energy changes in proteins upon ligand binding by NMR: Ca(2+) -displacement by Ln(3+) in a Ca(2+) -binding protein from Entamoeba histolytica.
Chem Biol Drug Des. 2011 Jan 14;
Authors: Chandra K, Mustafi SM, Muthukumar S, Chary KV
The study of protein-ligand interaction has been of a great interest in contemporary structural biology. The understanding of the nature...
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[NMR paper] Identification of the bile acid-binding site of the ileal lipid-binding protein by ph
Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
Related Articles Identification of the bile acid-binding site of the ileal lipid-binding protein by photoaffinity labeling, matrix-assisted laser desorption ionization-mass spectrometry, and NMR structure.
J Biol Chem. 2001 Mar 9;276(10):7291-301
Authors: Kramer W, Sauber K, Baringhaus KH, Kurz M, Stengelin S, Lange G, Corsiero D, Girbig F, König W, Weyland C
...
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[NMR paper] NMR solution structure of type II human cellular retinoic acid binding protein: impli
NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Related Articles NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding.
Biochemistry. 1998 Sep 15;37(37):12727-36
Authors: Wang L, Li Y, Abildgaard F, Markley JL, Yan H
The structure of human apo-cellular retinoic acid binding protein II (apo-CRABPII) in solution at pH 7.3 has been determined by NMR spectroscopy. The sequential assignments of the 1H, 13C, and 15N resonances...
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[NMR paper] NMR structure determination of the binding site for ribosomal protein S8 from Escheri
NMR structure determination of the binding site for ribosomal protein S8 from Escherichia coli 16 S rRNA.
Related Articles NMR structure determination of the binding site for ribosomal protein S8 from Escherichia coli 16 S rRNA.
J Mol Biol. 1998 Jul 24;280(4):639-54
Authors: Kalurachchi K, Nikonowicz EP
Many cellular processes involve the preferential interaction of an RNA molecule with a specific protein. A detailed analysis of the individual protein and RNA components of these interactions can provide unique insights into the structural...
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[NMR paper] 19F-NMR studies of retinol transfer between cellular retinol binding proteins and pho
19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles.
FEBS Lett. 1997 Feb 3;402(2-3):116-20
Authors: Rong D, Lin CL, d'Avignon DA, Lovey AJ, Rosenberger M, Li E
The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol...
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08-22-2010 03:31 PM
[NMR paper] 19F-NMR studies of retinol transfer between cellular retinol binding proteins and pho
19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--linkinghub.elsevier.com-ihub-images-PubMedLink.gif Related Articles 19F-NMR studies of retinol transfer between cellular retinol binding proteins and phospholipid vesicles.
FEBS Lett. 1997 Feb 3;402(2-3):116-20
Authors: Rong D, Lin CL, d'Avignon DA, Lovey AJ, Rosenberger M, Li E
The cellular retinol binding proteins, CRBP and CRBP II, are implicated in the cellular uptake of retinol...
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[NMR paper] An investigation of the ligand-binding site of the glutamine-binding protein of Esche
An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Related Articles An investigation of the ligand-binding site of the glutamine-binding protein of Escherichia coli using rotational-echo double-resonance NMR.
Biochemistry. 1994 Jul 26;33(29):8651-61
Authors: Hing AW, Tjandra N, Cottam PF, Schaefer J, Ho C
Glutamine-binding protein (GlnBP) is an essential component of the glutamine transport system in Escherichia coli. Rotational-echo double-resonance...
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[NMR paper] Inter-tryptophan distances in rat cellular retinol binding protein II by solid-state
Inter-tryptophan distances in rat cellular retinol binding protein II by solid-state NMR.
Related Articles Inter-tryptophan distances in rat cellular retinol binding protein II by solid-state NMR.
Biochemistry. 1993 May 4;32(17):4560-3
Authors: McDowell LM, Holl SM, Qian SJ, Li E, Schaefer J
Structural constraints for the tryptophans in rat cellular retinol binding protein II (CRBP II) have been obtained by rotational-echo double-resonance (REDOR) solid-state NMR. CRBP II was labeled with L-tryptophan and L-tryptophan. The 13C-19F dipolar...
Validation of the binding site structure of the cellular retinol-binding protein (CRB
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