메뉴 건너뛰기




Volumn 407, Issue 4, 2011, Pages 674-679

Structural analysis of the intracellular domain of (pro)renin receptor fused to maltose-binding protein

Author keywords

(Pro)renin receptor; ATP6ap2; Blood pressure; MBP fusion; RAS; Renin

Indexed keywords

DIMER; HYBRID PROTEIN; MALTOSE BINDING PROTEIN; MALTOSE BINDING PROTEIN PRORENIN RECEPTOR; MONOMER; MONOPHENOL MONOOXYGENASE; PRORENIN RECEPTOR; UNCLASSIFIED DRUG;

EID: 79955024105     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.03.074     Document Type: Article
Times cited : (12)

References (27)
  • 2
    • 0024603573 scopus 로고
    • A structural model to explain the partial catalytic activity of human prorenin
    • Heinrikson R.L., Hui J., Zurcher-Neely H., Poorman R.A. A structural model to explain the partial catalytic activity of human prorenin. Am. J. Hypertens. 1989, 2:367-380.
    • (1989) Am. J. Hypertens. , vol.2 , pp. 367-380
    • Heinrikson, R.L.1    Hui, J.2    Zurcher-Neely, H.3    Poorman, R.A.4
  • 3
    • 0025492620 scopus 로고
    • Protein modeling of human prorenin using the molecular dynamics method
    • Shiratori Y., Nakagawa S., Hori H., Murakami K., Umeyama H. Protein modeling of human prorenin using the molecular dynamics method. J. Mol. Graph. 1990, 8:163-167, 150.
    • (1990) J. Mol. Graph. , vol.8 , Issue.150 , pp. 163-167
    • Shiratori, Y.1    Nakagawa, S.2    Hori, H.3    Murakami, K.4    Umeyama, H.5
  • 4
    • 0036266596 scopus 로고    scopus 로고
    • Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin
    • Nguyen G., Delarue F., Burckle C., Bouzhir L., Giller T., Sraer J.D. Pivotal role of the renin/prorenin receptor in angiotensin II production and cellular responses to renin. J. Clin. Invest. 2002, 109:1417-1427.
    • (2002) J. Clin. Invest. , vol.109 , pp. 1417-1427
    • Nguyen, G.1    Delarue, F.2    Burckle, C.3    Bouzhir, L.4    Giller, T.5    Sraer, J.D.6
  • 5
    • 33750600468 scopus 로고    scopus 로고
    • Binding properties of rat prorenin and renin to the recombinant rat renin/prorenin receptor prepared by a baculovirus expression system
    • Nabi A.H., Kageshima A., Uddin M.N., Nakagawa T., Park E.Y., Suzuki F. Binding properties of rat prorenin and renin to the recombinant rat renin/prorenin receptor prepared by a baculovirus expression system. Int. J. Mol. Med. 2006, 18:483-488.
    • (2006) Int. J. Mol. Med. , vol.18 , pp. 483-488
    • Nabi, A.H.1    Kageshima, A.2    Uddin, M.N.3    Nakagawa, T.4    Park, E.Y.5    Suzuki, F.6
  • 6
    • 35848948398 scopus 로고    scopus 로고
    • Prorenin is the endogenous agonist of the (pro)renin receptor. Binding kinetics of renin and prorenin in rat vascular smooth muscle cells overexpressing the human (pro)renin receptor
    • Batenburg W.W., Krop M., Garrelds I.M., de Vries R., de Bruin R.J., Burckle C.A., Muller D.N., Bader M., Nguyen G., Danser A.H. Prorenin is the endogenous agonist of the (pro)renin receptor. Binding kinetics of renin and prorenin in rat vascular smooth muscle cells overexpressing the human (pro)renin receptor. J. Hypertens. 2007, 25:2441-2453.
    • (2007) J. Hypertens. , vol.25 , pp. 2441-2453
    • Batenburg, W.W.1    Krop, M.2    Garrelds, I.M.3    de Vries, R.4    de Bruin, R.J.5    Burckle, C.A.6    Muller, D.N.7    Bader, M.8    Nguyen, G.9    Danser, A.H.10
  • 8
    • 34347350179 scopus 로고    scopus 로고
    • Renin-stimulated TGF-beta1 expression is regulated by a mitogen-activated protein kinase in mesangial cells
    • Huang Y., Noble N.A., Zhang J., Xu C., Border W.A. Renin-stimulated TGF-beta1 expression is regulated by a mitogen-activated protein kinase in mesangial cells. Kidney Int. 2007, 72:45-52.
    • (2007) Kidney Int. , vol.72 , pp. 45-52
    • Huang, Y.1    Noble, N.A.2    Zhang, J.3    Xu, C.4    Border, W.A.5
  • 10
    • 30944469631 scopus 로고    scopus 로고
    • Renin increases mesangial cell transforming growth factor-beta1 matrix proteins through receptor-mediated angiotensin II-independent mechanisms
    • Huang Y., Wongamorntham S., Kasting J., McQuillan D., Owens R.T., Yu L., Noble N.A., Border W. Renin increases mesangial cell transforming growth factor-beta1 matrix proteins through receptor-mediated angiotensin II-independent mechanisms. Kidney Int. 2006, 69:105-113.
    • (2006) Kidney Int. , vol.69 , pp. 105-113
    • Huang, Y.1    Wongamorntham, S.2    Kasting, J.3    McQuillan, D.4    Owens, R.T.5    Yu, L.6    Noble, N.A.7    Border, W.8
  • 12
    • 75149152420 scopus 로고    scopus 로고
    • The biology of the (pro)renin receptor
    • Nguyen G., Muller D.N. The biology of the (pro)renin receptor. J. Am. Soc. Nephrol. 2010, 21:18-23.
    • (2010) J. Am. Soc. Nephrol. , vol.21 , pp. 18-23
    • Nguyen, G.1    Muller, D.N.2
  • 13
    • 75149122361 scopus 로고    scopus 로고
    • The (pro)renin receptor in health and disease
    • Nguyen G. The (pro)renin receptor in health and disease. Ann. Med. 2010, 42:13-18.
    • (2010) Ann. Med. , vol.42 , pp. 13-18
    • Nguyen, G.1
  • 15
    • 33845608395 scopus 로고    scopus 로고
    • A novel signal transduction cascade involving direct physical interaction of the renin/prorenin receptor with the transcription factor promyelocytic zinc finger protein
    • Schefe J.H., Menk M., Reinemund J., Effertz K., Hobbs R.M., Pandolfi P.P., Ruiz P., Unger T., Funke-Kaiser H. A novel signal transduction cascade involving direct physical interaction of the renin/prorenin receptor with the transcription factor promyelocytic zinc finger protein. Circ. Res. 2006, 99:1355-1366.
    • (2006) Circ. Res. , vol.99 , pp. 1355-1366
    • Schefe, J.H.1    Menk, M.2    Reinemund, J.3    Effertz, K.4    Hobbs, R.M.5    Pandolfi, P.P.6    Ruiz, P.7    Unger, T.8    Funke-Kaiser, H.9
  • 18
    • 0032079560 scopus 로고    scopus 로고
    • Identification characterization of a novel 9. 2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules
    • Ludwig J., Kerscher S., Brandt U., Pfeiffer K., Getlawi F., Apps D.K., Schagger H. Identification characterization of a novel 9. 2-kDa membrane sector-associated protein of vacuolar proton-ATPase from chromaffin granules. J. Biol. Chem. 1998, 273:10939-10947.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10939-10947
    • Ludwig, J.1    Kerscher, S.2    Brandt, U.3    Pfeiffer, K.4    Getlawi, F.5    Apps, D.K.6    Schagger, H.7
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Macromol. Crystallogr. 1997, Pt A276:307-326.
    • (1997) Macromol. Crystallogr. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 0028103275 scopus 로고
    • The CCP4 suite: programs for protein crystallography
    • The CCP4 suite: programs for protein crystallography. Acta. Crystallogr. D Biol. Crystallogr. 1994, 50:760-763.
    • (1994) Acta. Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 21
    • 0037154084 scopus 로고    scopus 로고
    • Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands
    • Duan X., Quiocho F.A. Structural evidence for a dominant role of nonpolar interactions in the binding of a transport/chemosensory receptor to its highly polar ligands. Biochemistry 2002, 41:706-712.
    • (2002) Biochemistry , vol.41 , pp. 706-712
    • Duan, X.1    Quiocho, F.A.2
  • 22
    • 0031571605 scopus 로고    scopus 로고
    • Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
    • Quiocho F.A., Spurlino J.C., Rodseth L.E. Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor. Structure 1997, 5:997-1015.
    • (1997) Structure , vol.5 , pp. 997-1015
    • Quiocho, F.A.1    Spurlino, J.C.2    Rodseth, L.E.3
  • 25
    • 0033551053 scopus 로고    scopus 로고
    • Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins
    • Kobe B., Center R.J., Kemp B.E., Poumbourios P. Crystal structure of human T cell leukemia virus type 1 gp21 ectodomain crystallized as a maltose-binding protein chimera reveals structural evolution of retroviral transmembrane proteins. Proc. Natl. Acad. Sci. USA 1999, 96:4319-4324.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4319-4324
    • Kobe, B.1    Center, R.J.2    Kemp, B.E.3    Poumbourios, P.4
  • 26
    • 34447255483 scopus 로고    scopus 로고
    • Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramers are essential for DNA mismatch repair in vivo
    • Mendillo M.L., Putnam C.D., Kolodner R.D. Escherichia coli MutS tetramerization domain structure reveals that stable dimers but not tetramers are essential for DNA mismatch repair in vivo. J. Biol. Chem. 2007, 282:16345-16354.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16345-16354
    • Mendillo, M.L.1    Putnam, C.D.2    Kolodner, R.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.