메뉴 건너뛰기




Volumn 296, Issue 2, 2000, Pages 341-349

Structure of human neutral endopeptidase (neprilysin) complexed with phosphoramidon

Author keywords

Endothelin converting enzyme; Enkephalinase; Metalloprotease; Phosphoramidon; X ray structure

Indexed keywords

ANALGESIC AGENT; ANTIHYPERTENSIVE AGENT; ATRIAL NATRIURETIC FACTOR; BRADYKININ; ENDOTHELIN; ENKEPHALIN; MEMBRANE METALLOENDOPEPTIDASE; PHOSPHORAMIDON; SUBSTANCE P;

EID: 0034681296     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1999.3492     Document Type: Article
Times cited : (256)

References (56)
  • 5
    • 0026597444 scopus 로고
    • Free R-value: A novel statistical quantity for assessing the accuracy of crystal structures
    • (1992) Nature , vol.355 , pp. 472-475
    • Brunger, A.T.1
  • 16
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme-2 is a membrane bound, phosphoramidon-sensitive metalloprotease with acidic pH optimum
    • (1995) J. Biol. Chem. , vol.270 , pp. 15262-15268
    • Emoto, N.1    Yanagisawa, M.2
  • 21
    • 0026908615 scopus 로고
    • Peptide mechanics: A force field for peptides and proteins working with entire residues as small units
    • (1992) Biopolymers , vol.32 , pp. 1003-1017
    • Gerber, P.1
  • 22
    • 0023038641 scopus 로고
    • Comparison of subsite specificity of the mammalian neutral endopeptidase 24.11 (enkephalinase) to the bacterial neutral endopeptidase thermolysin
    • (1986) J. Biol. Chem. , vol.261 , pp. 6433-6437
    • Hersh, L.B.1    Morihara, K.2
  • 23
    • 0030713349 scopus 로고    scopus 로고
    • Mutagenesis of Glu403 to Cys in rabbit neutral endopeptidase-24.11 (neprilysin) creates a disulphide-linked homodimer: Analogy with endothelin-converting enzyme
    • (1997) Biochem. J. , vol.327 , pp. 925-929
    • Hoang, M.V.1    Sansom, C.E.2    Turner, A.J.3
  • 24
    • 0028172551 scopus 로고
    • Protein hydration observed by X-ray diffraction. Solvation properties of penicillopepsin and neuraminidase crystal structures
    • (1994) J. Mol. Biol. , vol.243 , pp. 100-115
    • Jiang, J.S.1    Brunger, A.T.2
  • 25
    • 85046526624 scopus 로고
    • Evaluation of single crystal X-ray diffraction data from a position sensitive detector
    • (1988) J. Appl. Crystallog. , vol.21 , pp. 916-924
    • Kabsch, W.1
  • 27
    • 0015973588 scopus 로고
    • The purification and specicifity of a neutral endopeptidase from rabbit kidney brush border
    • (1974) Biochem. J. , vol.137 , pp. 477-488
    • Kerr, M.A.1    Kenny, A.J.2
  • 40
    • 33845280830 scopus 로고
    • Structural basis of the action of thermolysin and related zinc peptidases
    • (1988) Acc. Chem. Res. , vol.21 , pp. 333-340
    • Matthews, B.1
  • 42
    • 0007949705 scopus 로고
    • GRASP: Graphical Representation and Analysis of Surface Properties, Columbia University New York
    • (1992)
    • Nicholls, A.1    Honig, B.2
  • 43
    • 0002452464 scopus 로고
    • Oscillation data reduction program
    • Proceedings of the CCP4 Study Weekend: Data Collection and Processing (Wawyey, L., Isaacs, N. and Bailey, S., eds), SERC Daresbury Laboratory, Daresbury
    • (1993) , pp. 56-62
    • Otwinowski, Z.1
  • 54
    • 0029160578 scopus 로고
    • A gene PEX with homologies to endopeptidases is mutated in patients with X-linked hypophosphatemic rickets
    • The H.Y.P. Consortium
    • (1995) Nature Genet. , vol.11 , pp. 130-136


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.