메뉴 건너뛰기




Volumn 1813, Issue 10, 2011, Pages 1906-1916

Extracellular loops 1 and 3 and their associated transmembrane regions of the calcitonin receptor-like receptor are needed for CGRP receptor function

Author keywords

CGRP; Extracellular loop; G protein coupled receptor; Juxtamembrane domain; Receptor activation; Receptor activity modifying protein

Indexed keywords

ADENYLATE CYCLASE; ALANINE; ARGININE; CALCITONIN GENE RELATED PEPTIDE RECEPTOR; CALCITONIN RECEPTOR LIKE RECEPTOR; CYCLIC AMP; GLYCINE; HISTIDINE; LEUCINE; RHODOPSIN; VALINE;

EID: 80051801366     PISSN: 01674889     EISSN: 18792596     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2011.06.005     Document Type: Article
Times cited : (40)

References (32)
  • 1
    • 72749105799 scopus 로고    scopus 로고
    • Mapping interaction sites within the N-terminus of the calcitonin gene-related peptide receptor; the role of residues 23-60 of the calcitonin receptor-like receptor
    • Barwell J., Miller P.S., Donnelly D., Poyner D.R. Mapping interaction sites within the N-terminus of the calcitonin gene-related peptide receptor; the role of residues 23-60 of the calcitonin receptor-like receptor. Peptides 2010, 31:170-176.
    • (2010) Peptides , vol.31 , pp. 170-176
    • Barwell, J.1    Miller, P.S.2    Donnelly, D.3    Poyner, D.R.4
  • 2
    • 0030703626 scopus 로고    scopus 로고
    • Residues in the membrane-spanning and extracellular loop regions of the parathyroid hormone (PTH)-2 receptor determine signaling selectivity for PTH and PTH-related peptide
    • Bergwitz C., Jusseaume S.A., Luck M.D., Juppner H., Gardella T.J. Residues in the membrane-spanning and extracellular loop regions of the parathyroid hormone (PTH)-2 receptor determine signaling selectivity for PTH and PTH-related peptide. J. Biol. Chem. 1997, 272:28861-28868.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28861-28868
    • Bergwitz, C.1    Jusseaume, S.A.2    Luck, M.D.3    Juppner, H.4    Gardella, T.J.5
  • 3
    • 11244331476 scopus 로고    scopus 로고
    • A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors
    • Conner A.C., Hay D.L., Simms J., Howitt S.G., Schindler M., Smith D.M., et al. A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors. Mol. Pharmacol. 2005, 67:20-31.
    • (2005) Mol. Pharmacol. , vol.67 , pp. 20-31
    • Conner, A.C.1    Hay, D.L.2    Simms, J.3    Howitt, S.G.4    Schindler, M.5    Smith, D.M.6
  • 5
    • 49449095044 scopus 로고    scopus 로고
    • Functional and biophysical analysis of the C-terminus of the CGRP-receptor; a family B GPCR
    • Conner M., Hicks M.R., Dafforn T., Knowles T.J., Ludwig C., Staddon S., et al. Functional and biophysical analysis of the C-terminus of the CGRP-receptor; a family B GPCR. Biochemistry 2008, 47:8434-8444.
    • (2008) Biochemistry , vol.47 , pp. 8434-8444
    • Conner, M.1    Hicks, M.R.2    Dafforn, T.3    Knowles, T.J.4    Ludwig, C.5    Staddon, S.6
  • 6
    • 0032715220 scopus 로고    scopus 로고
    • Role of charged amino acids conserved in the vasoactive intestinal polypeptide/secretin family of receptors on the secretin receptor functionality
    • Di Paolo E., Vilardaga J.P., Petry H., Moguilevsky N., Bollen A., Robberecht P., et al. Role of charged amino acids conserved in the vasoactive intestinal polypeptide/secretin family of receptors on the secretin receptor functionality. Peptides 1999, 20:1187-1193.
    • (1999) Peptides , vol.20 , pp. 1187-1193
    • Di Paolo, E.1    Vilardaga, J.P.2    Petry, H.3    Moguilevsky, N.4    Bollen, A.5    Robberecht, P.6
  • 7
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky T.J., Czodrowski P., Li H., Nielsen J.E., Jensen J.H., Klebe G., et al. PDB2PQR: expanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res. 2007, 35:W522-W525.
    • (2007) Nucleic Acids Res. , vol.35
    • Dolinsky, T.J.1    Czodrowski, P.2    Li, H.3    Nielsen, J.E.4    Jensen, J.H.5    Klebe, G.6
  • 8
    • 69249087312 scopus 로고    scopus 로고
    • Juxtamembranous region of the amino terminus of the family B G protein-coupled calcitonin receptor plays a critical role in small-molecule agonist action
    • Dong M., Cox R.F., Miller L.J. Juxtamembranous region of the amino terminus of the family B G protein-coupled calcitonin receptor plays a critical role in small-molecule agonist action. J. Biol. Chem. 2009, 284:21839-21847.
    • (2009) J. Biol. Chem. , vol.284 , pp. 21839-21847
    • Dong, M.1    Cox, R.F.2    Miller, L.J.3
  • 9
    • 77951245644 scopus 로고    scopus 로고
    • Secretin occupies a single protomer of the homodimeric secretin receptor complex: insights from photoaffinity labeling studies using dual sites of covalent attachment
    • Dong M., Lam P.C., Pinon D.I., Orry A., Sexton P.M., Abagyan R., et al. Secretin occupies a single protomer of the homodimeric secretin receptor complex: insights from photoaffinity labeling studies using dual sites of covalent attachment. J. Biol. Chem. 2010, 285:9919-9931.
    • (2010) J. Biol. Chem. , vol.285 , pp. 9919-9931
    • Dong, M.1    Lam, P.C.2    Pinon, D.I.3    Orry, A.4    Sexton, P.M.5    Abagyan, R.6
  • 10
    • 0031566170 scopus 로고    scopus 로고
    • Aspartate 196 in the first extracellular loop of the human VIP1 receptor is essential for VIP binding and VIP-stimulated cAMP production
    • Du K., Nicole P., Couvineau A., Laburthe M. Aspartate 196 in the first extracellular loop of the human VIP1 receptor is essential for VIP binding and VIP-stimulated cAMP production. Biochem. Biophys. Res. Commun. 1997, 230:289-292.
    • (1997) Biochem. Biophys. Res. Commun. , vol.230 , pp. 289-292
    • Du, K.1    Nicole, P.2    Couvineau, A.3    Laburthe, M.4
  • 11
    • 71549119499 scopus 로고    scopus 로고
    • Molecular basis of association of receptor activity-modifying protein 3 with the family B G protein-coupled secretin receptor
    • Harikumar K.G., Simms J., Christopoulos G., Sexton P.M., Miller L.J. Molecular basis of association of receptor activity-modifying protein 3 with the family B G protein-coupled secretin receptor. Biochemistry 2009, 48:11773-11785.
    • (2009) Biochemistry , vol.48 , pp. 11773-11785
    • Harikumar, K.G.1    Simms, J.2    Christopoulos, G.3    Sexton, P.M.4    Miller, L.J.5
  • 12
    • 0035834719 scopus 로고    scopus 로고
    • Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestin
    • Hilairet S., Belanger C., Bertrand J., Laperriere A., Foord S.M., Bouvier M. Agonist-promoted internalization of a ternary complex between calcitonin receptor-like receptor, receptor activity-modifying protein 1 (RAMP1), and beta-arrestin. J. Biol. Chem. 2001, 276:42182-42190.
    • (2001) J. Biol. Chem. , vol.276 , pp. 42182-42190
    • Hilairet, S.1    Belanger, C.2    Bertrand, J.3    Laperriere, A.4    Foord, S.M.5    Bouvier, M.6
  • 13
    • 15844385219 scopus 로고    scopus 로고
    • Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor
    • Holtmann M.H., Ganguli S., Hadac E.M., Dolu V., Miller L.J. Multiple extracellular loop domains contribute critical determinants for agonist binding and activation of the secretin receptor. J. Biol. Chem. 1996, 271:14944-14949.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14944-14949
    • Holtmann, M.H.1    Ganguli, S.2    Hadac, E.M.3    Dolu, V.4    Miller, L.J.5
  • 14
    • 0242322528 scopus 로고    scopus 로고
    • An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins
    • Im W., Feig M., Brooks C.L. An implicit membrane generalized born theory for the study of structure, stability, and interactions of membrane proteins. Biophys. J. 2003, 85:2900-2918.
    • (2003) Biophys. J. , vol.85 , pp. 2900-2918
    • Im, W.1    Feig, M.2    Brooks, C.L.3
  • 15
    • 0037247242 scopus 로고    scopus 로고
    • Lysine 195 and aspartate 196 in the first extracellular loop of the VPAC1 receptor are essential for high affinity binding of agonists but not of antagonists
    • Langer I., Vertongen P., Perret J., Waelbroeck M., Robberecht P. Lysine 195 and aspartate 196 in the first extracellular loop of the VPAC1 receptor are essential for high affinity binding of agonists but not of antagonists. Neuropharmacology 2003, 44:125-131.
    • (2003) Neuropharmacology , vol.44 , pp. 125-131
    • Langer, I.1    Vertongen, P.2    Perret, J.3    Waelbroeck, M.4    Robberecht, P.5
  • 16
    • 0035175679 scopus 로고    scopus 로고
    • PDBsum: summaries and analyses of PDB structures
    • Laskowski R.A. PDBsum: summaries and analyses of PDB structures. Nucleic Acids Res. 2001, 29:221-222.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 221-222
    • Laskowski, R.A.1
  • 17
    • 0027169515 scopus 로고
    • Main-chain bond lengths and bond angles in protein structures
    • Laskowski R.A., Moss D.S., Thornton J.M. Main-chain bond lengths and bond angles in protein structures. J. Mol. Biol. 1993, 231:1049-1067.
    • (1993) J. Mol. Biol. , vol.231 , pp. 1049-1067
    • Laskowski, R.A.1    Moss, D.S.2    Thornton, J.M.3
  • 18
    • 28644432877 scopus 로고    scopus 로고
    • Very fast empirical prediction and rationalization of protein pKa values
    • Li H., Robertson A.D., Jensen J.H. Very fast empirical prediction and rationalization of protein pKa values. Proteins 2005, 61:704-721.
    • (2005) Proteins , vol.61 , pp. 704-721
    • Li, H.1    Robertson, A.D.2    Jensen, J.H.3
  • 19
    • 0032574982 scopus 로고    scopus 로고
    • RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor
    • McLatchie L.M., Fraser N.J., Main M.J., Wise A., Brown J., Thompson N., et al. RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor. Nature 1998, 393:333-339.
    • (1998) Nature , vol.393 , pp. 333-339
    • McLatchie, L.M.1    Fraser, N.J.2    Main, M.J.3    Wise, A.4    Brown, J.5    Thompson, N.6
  • 20
    • 79955540676 scopus 로고    scopus 로고
    • Refinement of glucagon-like peptide 1 docking to its intact receptor using mid-region photolabile probes and molecular modeling
    • Miller L.J., Chen Q., Lam P.C., Pinon D.I., Sexton P.M., Abagyan R., et al. Refinement of glucagon-like peptide 1 docking to its intact receptor using mid-region photolabile probes and molecular modeling. J. Biol. Chem. 2011, 286:15895-15907.
    • (2011) J. Biol. Chem. , vol.286 , pp. 15895-15907
    • Miller, L.J.1    Chen, Q.2    Lam, P.C.3    Pinon, D.I.4    Sexton, P.M.5    Abagyan, R.6
  • 22
    • 67149136711 scopus 로고    scopus 로고
    • Passing the baton in class B GPCRs: peptide hormone activation via helix induction?
    • Parthier C., Reedtz-Runge S., Rudolph R., Stubbs M.T. Passing the baton in class B GPCRs: peptide hormone activation via helix induction?. Trends Biochem. Sci. 2009, 34:303-310.
    • (2009) Trends Biochem. Sci. , vol.34 , pp. 303-310
    • Parthier, C.1    Reedtz-Runge, S.2    Rudolph, R.3    Stubbs, M.T.4
  • 23
    • 78650919353 scopus 로고    scopus 로고
    • Importance of the extracellular loops in G protein-coupled receptors for ligand recognition and receptor activation
    • Peeters M.C., van Westen G.J., Li Q., Ijzerman A.P. Importance of the extracellular loops in G protein-coupled receptors for ligand recognition and receptor activation. Trends Pharmacol. Sci. 2011, 32:35-42.
    • (2011) Trends Pharmacol. Sci. , vol.32 , pp. 35-42
    • Peeters, M.C.1    van Westen, G.J.2    Li, Q.3    Ijzerman, A.P.4
  • 25
    • 0041344589 scopus 로고    scopus 로고
    • Three distinct epitopes on the extracellular face of the glucagon receptor determine specificity for the glucagon amino terminus
    • Runge S., Gram C., Brauner-Osborne H., Madsen K., Knudsen L.B., Wulff B.S. Three distinct epitopes on the extracellular face of the glucagon receptor determine specificity for the glucagon amino terminus. J. Biol. Chem. 2003, 278:28005-28010.
    • (2003) J. Biol. Chem. , vol.278 , pp. 28005-28010
    • Runge, S.1    Gram, C.2    Brauner-Osborne, H.3    Madsen, K.4    Knudsen, L.B.5    Wulff, B.S.6
  • 26
    • 0033546197 scopus 로고    scopus 로고
    • Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation
    • Sheikh S.P., Vilardarga J.P., Baranski T.J., Lichtarge O., Iiri T., Meng E.C., et al. Similar structures and shared switch mechanisms of the beta2-adrenoceptor and the parathyroid hormone receptor. Zn(II) bridges between helices III and VI block activation. J. Biol. Chem. 1999, 274:17033-17041.
    • (1999) J. Biol. Chem. , vol.274 , pp. 17033-17041
    • Sheikh, S.P.1    Vilardarga, J.P.2    Baranski, T.J.3    Lichtarge, O.4    Iiri, T.5    Meng, E.C.6
  • 29
    • 77956336134 scopus 로고    scopus 로고
    • Crystal structure of the ectodomain complex of the CGRP receptor, a class-B GPCR, reveals the site of drug antagonism
    • ter Haar E., Koth C.M., Abdul-Manan N., Swenson L., Coll J.T., Lippke J.A., et al. Crystal structure of the ectodomain complex of the CGRP receptor, a class-B GPCR, reveals the site of drug antagonism. Structure 2010, 18:1083-1093.
    • (2010) Structure , vol.18 , pp. 1083-1093
    • ter Haar, E.1    Koth, C.M.2    Abdul-Manan, N.3    Swenson, L.4    Coll, J.T.5    Lippke, J.A.6
  • 31
    • 0037188507 scopus 로고    scopus 로고
    • Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction
    • Xiang Z., Soto C.S., Honig B. Evaluating conformational free energies: the colony energy and its application to the problem of loop prediction. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:7432-7437.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 7432-7437
    • Xiang, Z.1    Soto, C.S.2    Honig, B.3
  • 32
    • 79954782236 scopus 로고    scopus 로고
    • Structure of an agonist-bound human A2A adenosine receptor
    • Xu F., Wu H., Katritch V., Han G.W., Jacobson K.A., Gao Z.G., et al. Structure of an agonist-bound human A2A adenosine receptor. Science 2011, 332:322-327.
    • (2011) Science , vol.332 , pp. 322-327
    • Xu, F.1    Wu, H.2    Katritch, V.3    Han, G.W.4    Jacobson, K.A.5    Gao, Z.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.