Binding of retinol induces changes in rat cellular retinol-binding protein II conformation and backbone dynamics

Journal of Molecular Biology

Volumn 300, Issue 3, 2000, Pages 619-632

  Lu, J ^a   Lin, C L ^a   Tang, C ^a   Ponder, J W ^a   Kao, J L F ^a   Cistola, D P ^a   Li, E ^a  

^a WASHINGTON UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

Cellular retinol binding protein; Lipid transport; Lipid binding protein; NMR; Structure

Indexed keywords

CELLULAR RETINOL BINDING PROTEIN; LIGAND; LIPID BINDING PROTEIN; POLYPEPTIDE; RETINOL;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTON TRANSPORT; RAT; X RAY ANALYSIS;

EID: 0034647414     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.2000.3883     Document Type: Article

References (37)

1. 13C-enriched proteins
2. Generation of cellular retinol binding protein II in knockout mice
3. 15N NMR relaxation
4. Cellular retinol-binding protein I is essential for vitamin A homeostasis
5. Torsion-angle dynamics for NMR structure calculation with the new program DYANA
6. 13C NMR detection of a perturbed 6-s-trans chromophore in bacteriorhodopsin
7. Differential interaction of lecithin-retinol acyltransferase with cellular retinol binding proteins
8. Differential mechanisms of retinoid transfer from cellular retinol binding proteins types I and II to phospholipid membranes
9. Discrete backbone disorder in the NMR structure of apo intestinal fatty acid-binding protein in solution: Implications for the mechanism of ligand entry
10. 1H exchange
11. The NMR solution structure of intestinal fatty acid-binding protein complexed with palmitate: Application of a novel distance geometry algorithm
12. Ring orientation in β-Ionone and retinals
13. Cellular retinoid-binding proteins: Limited proteolysis reveals a conformational change upon ligand binding
14. 2O
15. 13C-labeled proteins
16. MOLMOL: A program for display and analysis of macromolecular structures
17. PROCHECK: A program to check the stereochemical quality of protein structures
18. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
19. Structure/function of cytoplasmic vitamin A-binding proteins
20. Fluorine nuclear magnetic resonance analysis of the ligand binding properties of two homologous, rat cellular retinol-binding proteins expressed in Escherichia coli
21. Photochemistry and synthesis of stereoisomers of vitamin A
22. The structure and dynamics of rat apo-cellular retinol-binding protein II in solution: Comparison with the X-ray structure
23. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
24. Quantitative analyses of naturally occurring retinoids
25. Nuclear magnetic resonance studies demonstrate differences in the interaction of retinoic acid with two highly homologous cellular retinoic acid binding proteins
26. An improved double-tuned and isotope-filtered pulse scheme based on a pulsed field gradient and a wide-band inversion shaped pulse
27. Cellular retinoid binding proteins
28. Pilus chaperone FimC-adhesin FimH interactions mapped by TROSY-NMR
29. Holo-cellular retinol-binding protein: Distinction of ligand-binding affinity from efficiency as substrate in retinal biosynthesis
30. 15N-enriched proteins using constant-time evolution
31. Differential binding of retinol analogs to two homologous cellular retinol-binding proteins
32. 15N isotope editing of biomolecular complexes. Application to a mutant Lac repressor headpiece DNA complex
33. Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation
34. Essential dynamics of the cellular retinol-binding protein evidence for ligand-induced conformational changes
35. Crystal structures of holo and apo-cellular retinol-binding protein II
36. 13C chemical-shift data
37. 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques