메뉴 건너뛰기




Volumn 11, Issue 12, 2003, Pages 1521-1526

Crystal Structure of a μ-like Calpain Reveals a Partially Activated Conformation with Low Ca2+ Requirement

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; CALPAIN; CYSTEINE; HISTIDINE; MU CALPAIN; MU-CALPAIN;

EID: 3442884354     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.str.2003.11.007     Document Type: Article
Times cited : (25)

References (26)
  • 1
    • 0029165075 scopus 로고
    • Active site residues in m-calpain: Identification by site-directed mutagenesis
    • Arthur J.S., Gauthier S., Elce J.S. Active site residues in m-calpain. identification by site-directed mutagenesis FEBS Lett. 368:1995;397-400.
    • (1995) FEBS Lett. , vol.368 , pp. 397-400
    • Arthur, J.S.1    Gauthier, S.2    Elce, J.S.3
  • 2
    • 0034116930 scopus 로고    scopus 로고
    • Disruption of the murine calpain small subunit gene, Capn4: Calpain is essential for embryonic development but not for cell growth and division
    • Arthur J.S., Elce J.S., Hegadorn C., Williams K., Greer P.A. Disruption of the murine calpain small subunit gene, Capn4. calpain is essential for embryonic development but not for cell growth and division Mol. Cell. Biol. 20:2000;4474-4481.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 4474-4481
    • Arthur, J.S.1    Elce, J.S.2    Hegadorn, C.3    Williams, K.4    Greer, P.A.5
  • 4
    • 0030998285 scopus 로고    scopus 로고
    • Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes
    • Blanchard H., Grochulski P., Li Y., Arthur J.S., Davies P.L., Elce J.S., Cygler M. Structure of a calpain Ca(2+)-binding domain reveals a novel EF-hand and Ca(2+)-induced conformational changes. Nat. Struct. Biol. 4:1997;532-553.
    • (1997) Nat. Struct. Biol. , vol.4 , pp. 532-553
    • Blanchard, H.1    Grochulski, P.2    Li, Y.3    Arthur, J.S.4    Davies, P.L.5    Elce, J.S.6    Cygler, M.7
  • 5
    • 0029930588 scopus 로고    scopus 로고
    • Contribution to activity of histidine-aromatic, amide-aromatic, and aromatic-aromatic interactions in the extended catalytic site of cysteine proteinases
    • Bromme D., Bonneau P.R., Purisima E., Lachance P., Hajnik S., Thomas D.Y., Storer A.C. Contribution to activity of histidine-aromatic, amide-aromatic, and aromatic-aromatic interactions in the extended catalytic site of cysteine proteinases. Biochemistry. 35:1996;3970-3979.
    • (1996) Biochemistry , vol.35 , pp. 3970-3979
    • Bromme, D.1    Bonneau, P.R.2    Purisima, E.3    Lachance, P.4    Hajnik, S.5    Thomas, D.Y.6    Storer, A.C.7
  • 7
    • 0028103275 scopus 로고
    • The CCP4 (Collaborative Computational Project 4) suite: Programs for protein crystallography
    • CCP4 The CCP4 (Collaborative Computational Project 4) suite. programs for protein crystallography Acta Crystallogr. D. 50:1994;760-763.
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 8
    • 0035934230 scopus 로고    scopus 로고
    • Identification and characterization of two novel calpain large subunit genes
    • Dear T.N., Boehm T. Identification and characterization of two novel calpain large subunit genes. Gene. 274:2001;245-252.
    • (2001) Gene , vol.274 , pp. 245-252
    • Dear, T.N.1    Boehm, T.2
  • 9
    • 0034657159 scopus 로고    scopus 로고
    • Roles of individual EF-hands in the activation of m-calpain by calcium
    • Dutt P., Arthur J.S., Grochulski P., Cygler M., Elce J.S. Roles of individual EF-hands in the activation of m-calpain by calcium. Biochem. J. 348:2000;37-43.
    • (2000) Biochem. J. , vol.348 , pp. 37-43
    • Dutt, P.1    Arthur, J.S.2    Grochulski, P.3    Cygler, M.4    Elce, J.S.5
  • 10
    • 0036796233 scopus 로고    scopus 로고
    • Origins of the difference in Ca2+ requirement for activation of mu- and m-calpain
    • Dutt P., Spriggs C.N., Davies P.L., Jia Z., Elce J.S. Origins of the difference in Ca2+ requirement for activation of mu- and m-calpain. Biochem. J. 367:2002;263-269.
    • (2002) Biochem. J. , vol.367 , pp. 263-269
    • Dutt, P.1    Spriggs, C.N.2    Davies, P.L.3    Jia, Z.4    Elce, J.S.5
  • 11
    • 79952608525 scopus 로고
    • Accurate bond and angle parameters for X-ray protein structure refinement
    • Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A. 47:1991;392-400.
    • (1991) Acta Crystallogr. a , vol.47 , pp. 392-400
    • Engh, R.A.1    Huber, R.2
  • 13
    • 0033573028 scopus 로고    scopus 로고
    • Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation
    • Hosfield C.M., Elce J.S., Davies P.L., Jia Z. Crystal structure of calpain reveals the structural basis for Ca(2+)-dependent protease activity and a novel mode of enzyme activation. EMBO J. 18:1999;6880-6889.
    • (1999) EMBO J. , vol.18 , pp. 6880-6889
    • Hosfield, C.M.1    Elce, J.S.2    Davies, P.L.3    Jia, Z.4
  • 14
    • 0033557766 scopus 로고    scopus 로고
    • Structural basis of profactor D activation: From a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D
    • Jing H., Macon K.J., Moore D., DeLucas L.J., Volanakis J.E., Narayana S.V. Structural basis of profactor D activation. from a highly flexible zymogen to a novel self-inhibited serine protease, complement factor D EMBO J. 18:1999;804-814.
    • (1999) EMBO J. , vol.18 , pp. 804-814
    • Jing, H.1    MacOn, K.J.2    Moore, D.3    Delucas, L.J.4    Volanakis, J.E.5    Narayana, S.V.6
  • 16
    • 0037386530 scopus 로고    scopus 로고
    • Calpain regulates the crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium neutrophil chemotaxis
    • Lokuta M.A., Nuzzi P.A., Huttenlocher A. Calpain regulates the crystal structure of calcium-free human m-calpain suggests an electrostatic switch mechanism for activation by calcium neutrophil chemotaxis. Proc. Natl. Acad. Sci. USA. 100:2003;4006-4011.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4006-4011
    • Lokuta, M.A.1    Nuzzi, P.A.2    Huttenlocher, A.3
  • 17
    • 0002705842 scopus 로고
    • A visual protein crystallographic software system for X11/XView
    • McRee D.E. A visual protein crystallographic software system for X11/XView. J. Mol. Graph. 10:1992;44-46.
    • (1992) J. Mol. Graph. , vol.10 , pp. 44-46
    • McRee, D.E.1
  • 22
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinoski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinoski, Z.1    Minor, W.2
  • 23
    • 0035861569 scopus 로고    scopus 로고
    • Dissociation and aggregation of calpain in the presence of calcium
    • Pal G.P., Elce J.S., Jia Z. Dissociation and aggregation of calpain in the presence of calcium. J. Biol. Chem. 276:2001;47233-47238.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47233-47238
    • Pal, G.P.1    Elce, J.S.2    Jia, Z.3
  • 24
    • 0037321565 scopus 로고    scopus 로고
    • Purification, crystallization and preliminary X-ray analysis of a mu-like calpain
    • Pal G.P., DeVeyra T., Elce J.S., Jia Z. Purification, crystallization and preliminary X-ray analysis of a mu-like calpain. Acta Crystallogr. D. 59:2003;369-371.
    • (2003) Acta Crystallogr. D , vol.59 , pp. 369-371
    • Pal, G.P.1    Deveyra, T.2    Elce, J.S.3    Jia, Z.4
  • 25
    • 0034992155 scopus 로고    scopus 로고
    • The structure of calpain
    • Sorimachi H., Suzuki K. The structure of calpain. J. Biochem. 129:2001;653-664.
    • (2001) J. Biochem. , vol.129 , pp. 653-664
    • Sorimachi, H.1    Suzuki, K.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.