Conformational Changes in the Parathyroid Hormone Receptor Associated with Activation by Agonist
Author:
Affiliation:
1. Department of Physiology (B.E.T., I.W., A.W., M.R.), Tufts University School of Medicine, Boston, Massachusetts 02111
2. Department of Chemistry (D.F.M.), Dartmouth College, Hanover, New Hampshire 03755
Publisher
The Endocrine Society
Subject
Endocrinology,Molecular Biology,General Medicine
Link
http://academic.oup.com/mend/article-pdf/22/5/1154/8938527/mend1154.pdf
Reference38 articles.
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2. Klein-Seetharaman J, Yanamala NV, Javeed F, Reeves PJ, Getmanova EV, Loewen MC, Schwalbe H, Khorana HG 2004Differential dynamics in the G protein-coupled receptor rhodopsin revealed by solution NMR.Proc Natl Acad Sci USA101:3409–3413
3. Klein-Seetharaman J, Hwa J, Cai K, Altenbach C, Hubbell WL, Khorana HG 2001Probing the dark state tertiary structure in the cytoplasmic domain of rhodopsin: proximities between amino acids deduced from spontaneous disulfide bond formation between Cys316 and engineered cysteines in cytoplasmic loop 1.Biochemistry40:12472–12478
4. Altenbach C, Cai K, Klein-Seetharaman J, Khorana HG, Hubbell WL 2001Structure and function in rhodopsin: mapping light-dependent changes in distance between residue 65 in helix TM1 and residues in the sequence 306–319 at the cytoplasmic end of helix TM7 and in helix H8.Biochemistry40:15483–15492
5. Hubbell WL, Cafiso DS, Altenbach C Identifying conformational changes with site-directed spin labeling, Nat Struct Biol 2000 7:735–739
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2. Kinetic and Thermodynamic Insights on Agonist Interactions with the Parathyroid Hormone Receptor-1 from a New NanoBRET assay;2022-07-25
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