دورية أكاديمية
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NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1.

التفاصيل البيبلوغرافية
العنوان: NMR exchange broadening arising from specific low affinity protein self-association: analysis of nitrogen-15 nuclear relaxation for rat CD2 domain 1.
المؤلفون: Pfuhl M; Department of Biochemistry and Molecular Biology, University College London, U.K., Chen HA, Kristensen SM, Driscoll PC
المصدر: Journal of biomolecular NMR [J Biomol NMR] 1999 Aug; Vol. 14 (4), pp. 307-20.
نوع المنشور: Journal Article; Research Support, Non-U.S. Gov't
اللغة: English
بيانات الدورية: Publisher: Springer Country of Publication: Netherlands NLM ID: 9110829 Publication Model: Print Cited Medium: Print ISSN: 0925-2738 (Print) Linking ISSN: 09252738 NLM ISO Abbreviation: J Biomol NMR Subsets: MEDLINE
أسماء مطبوعة: Publication: <2005->: Leiden, The Netherlands : Springer
Original Publication: Leiden, The Netherlands : ESCOM Science Publishers, c1991-
مواضيع طبية MeSH: CD2 Antigens/*chemistry, Animals ; Dimerization ; Magnetic Resonance Spectroscopy ; Nitrogen ; Rats
مستخلص: Nuclear spin relaxation monitored by heteronuclear NMR provides a useful method to probe the overall and internal molecular motion for biological macromolecules over a variety of time scales. Nitrogen-15 NMR relaxation parameters have been recorded for the N-terminal domain of the rat T-cell antigen CD2 (CD2d1) in a dilution series from 1.20 mM to 40 microM (pH 6.0, 25 degrees C). The data have been analysed within the framework of the model-free formalism of Lipari and Szabo to understand the molecular origin of severely enhanced transverse relaxation rates found for certain residues. These data revealed a strong dependence of the derived molecular correlation time tau c upon the CD2d1 protein concentration. Moreover, a number of amide NH resonances exhibited exchange broadening and chemical shifts both strongly dependent on protein concentration. These amide groups cluster on the major beta-sheet surface of CD2d1 that coincides with a major lattice contact in the X-ray structure of the intact ectodomain of rat CD2. The complete set of relaxation data fit well to an equilibrium monomer-dimer exchange model, yielding estimates of exchange rate constants (kON = 5000 M-1 s-1; kOFF = 7 s-1) and a dissociation constant (KD approximately 3-6 mM) that is consistent with the difficulty in detecting the weak interactions for this molecule by alternative biophysical methods. The self-association of CD2d1 is essentially invariant to changes in buffer composition and ionic strength and the associated relaxation phenomena cannot be explained as a result of neglecting anisotropic rotational diffusion in the analysis. These observations highlight the necessity to consider low affinity protein self-association interactions as a source of residue specific exchange phenomena in NMR spectra of macromolecular biomolecules, before the assignment of more elaborate intramolecular conformational mechanisms.
References: Nat Struct Biol. 1998 Jan;5(1):55-9. (PMID: 9437430)
Protein Sci. 1997 Mar;6(3):534-42. (PMID: 9070436)
J Biomol NMR. 1995 Jul;6(1):1-10. (PMID: 22911575)
Biochemistry. 1989 Jan 10;28(1):362-70. (PMID: 2706262)
J Biomol NMR. 1995 Nov;6(3):277-93. (PMID: 8520220)
Nature. 1991 Oct 24;353(6346):762-5. (PMID: 1682812)
Biochemistry. 1998 May 19;37(20):7119-26. (PMID: 9585523)
J Biomol NMR. 1993 Mar;3(2):151-64. (PMID: 7682879)
Q Rev Biophys. 1981 Feb;14(1):81-139. (PMID: 7025081)
Biochem Soc Trans. 1993 Nov;21(4):947-52. (PMID: 7907561)
Nature. 1992 Nov 19;360(6401):232-9. (PMID: 1279440)
Biochemistry. 1998 May 19;37(20):7617-29. (PMID: 9585577)
J Biomol NMR. 1998 Jul;12(1):177-82. (PMID: 20700691)
J Biomol NMR. 1998 Aug;12(2):307-18. (PMID: 9752001)
J Biomol NMR. 1994 May;4(3):341-8. (PMID: 8019141)
J Biomol NMR. 1997 Apr;9(3):287-98. (PMID: 9204557)
J Mol Biol. 1996 Oct 25;263(2):369-82. (PMID: 8913313)
Protein Sci. 1997 Jun;6(6):1248-63. (PMID: 9194185)
Biochemistry. 1992 Jun 16;31(23):5269-78. (PMID: 1606151)
Biochemistry. 1998 Aug 4;37(31):10906-19. (PMID: 9692983)
Biochemistry. 1989 Nov 14;28(23):8972-9. (PMID: 2690953)
Biochemistry. 1996 May 14;35(19):5982-91. (PMID: 8634239)
Biophys J. 1994 Aug;67(2):530-1. (PMID: 7948671)
Methods Enzymol. 1994;239:596-619. (PMID: 7830600)
Eur Biophys J. 1997;25(5-6):455-62. (PMID: 9188168)
Structure. 1994 Aug 15;2(8):755-66. (PMID: 7994575)
J Mol Biol. 1997 May 2;268(2):494-511. (PMID: 9159486)
J Biomol NMR. 1997 Dec;10(4):363-72. (PMID: 20859782)
Proc Natl Acad Sci U S A. 1998 Aug 18;95(17):9897-902. (PMID: 9707572)
J Mol Biol. 1998 Jul 31;280(5):879-96. (PMID: 9671557)
J Mol Biol. 1997 Feb 14;266(1):173-94. (PMID: 9054979)
Nat Struct Biol. 1998 Jul;5 Suppl:513-7. (PMID: 9665181)
J Magn Reson. 1998 Apr;131(2):351-7. (PMID: 9571112)
Prog Biophys Mol Biol. 1996;65(3):171-219. (PMID: 9062432)
J Biomol NMR. 1996 Oct;8(3):273-84. (PMID: 8953218)
J Mol Biol. 1995 Feb 10;246(1):144-63. (PMID: 7531772)
J Biomol NMR. 1998 Oct;12(3):457-8. (PMID: 9835053)
Biochemistry. 1990 Aug 14;29(32):7387-401. (PMID: 2223770)
Immunol Rev. 1998 Jun;163:217-36. (PMID: 9700513)
Biochemistry. 1993 Apr 13;32(14):3571-82. (PMID: 7682109)
المشرفين على المادة: 0 (CD2 Antigens)
N762921K75 (Nitrogen)
تواريخ الأحداث: Date Created: 19991020 Date Completed: 19991102 Latest Revision: 20190921
رمز التحديث: 20231215
DOI: 10.1023/a:1008319917267
PMID: 10526406
قاعدة البيانات: MEDLINE
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