메뉴 건너뛰기




Volumn 584, Issue 5, 2010, Pages 878-882

Crystal structure of the LMAN1-CRD/MCFD2 transport receptor complex provides insight into combined deficiency of factor V and factor VIII

Author keywords

Crystal structure; ER quality control; ERGIC 53; Glycoprotein transport; Protein complex

Indexed keywords

BLOOD CLOTTING FACTOR 5; BLOOD CLOTTING FACTOR 8; GLYCOPROTEIN; PROTEIN LMAN1; PROTEIN MCFD2; UNCLASSIFIED DRUG;

EID: 76749118043     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2010.02.009     Document Type: Article
Times cited : (23)

References (25)
  • 1
    • 19444368098 scopus 로고
    • Congenital factor V deficiency (parahemophilia) with true hemophilia in two brothers
    • Oeri J. Congenital factor V deficiency (parahemophilia) with true hemophilia in two brothers. Bibl. Paediatr. 58 (1954) 575-588
    • (1954) Bibl. Paediatr. , vol.58 , pp. 575-588
    • Oeri, J.1
  • 5
    • 21844438479 scopus 로고    scopus 로고
    • LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway
    • Zhang B., Kaufman R.J., and Ginsburg D. LMAN1 and MCFD2 form a cargo receptor complex and interact with coagulation factor VIII in the early secretory pathway. J. Biol. Chem. 280 (2005) 25881-25886
    • (2005) J. Biol. Chem. , vol.280 , pp. 25881-25886
    • Zhang, B.1    Kaufman, R.J.2    Ginsburg, D.3
  • 6
    • 41349121801 scopus 로고    scopus 로고
    • The sugar-binding ability of ERGIC-53 is enhanced by its interaction with MCFD2
    • Kawasaki N., Ichikawa Y., Matsuo I., Totani K., Matsumoto N., Ito Y., and Yamamoto K. The sugar-binding ability of ERGIC-53 is enhanced by its interaction with MCFD2. Blood 111 (2008) 1972-1979
    • (2008) Blood , vol.111 , pp. 1972-1979
    • Kawasaki, N.1    Ichikawa, Y.2    Matsuo, I.3    Totani, K.4    Matsumoto, N.5    Ito, Y.6    Yamamoto, K.7
  • 7
    • 48449089504 scopus 로고    scopus 로고
    • New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2
    • Guy J.E., Wigren E., Svärd M., Härd T., and Lindqvist Y. New insights into multiple coagulation factor deficiency from the solution structure of human MCFD2. J. Mol. Biol. 381 (2008) 941-955
    • (2008) J. Mol. Biol. , vol.381 , pp. 941-955
    • Guy, J.E.1    Wigren, E.2    Svärd, M.3    Härd, T.4    Lindqvist, Y.5
  • 8
    • 0033202958 scopus 로고    scopus 로고
    • The lectin ERGIC-53 is a cargo transport receptor for glycoproteins
    • Appenzeller C., Andersson H., Kappeler F., and Hauri H.P. The lectin ERGIC-53 is a cargo transport receptor for glycoproteins. Nat. Cell Biol. 1 (1999) 330-334
    • (1999) Nat. Cell Biol. , vol.1 , pp. 330-334
    • Appenzeller, C.1    Andersson, H.2    Kappeler, F.3    Hauri, H.P.4
  • 9
    • 27744508476 scopus 로고    scopus 로고
    • Oligomerization and intracellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds
    • Neve E.P.A., Lahtinen U., and Pettersson R.F. Oligomerization and intracellular localization of the glycoprotein receptor ERGIC-53 is independent of disulfide bonds. J. Mol. Biol. 354 (2005) 556-568
    • (2005) J. Mol. Biol. , vol.354 , pp. 556-568
    • Neve, E.P.A.1    Lahtinen, U.2    Pettersson, R.F.3
  • 10
    • 33745485316 scopus 로고    scopus 로고
    • The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function
    • Appenzeller-Herzog C., and Hauri H.P. The ER-Golgi intermediate compartment (ERGIC): in search of its identity and function. J. Cell Sci. 119 (2006) 2173-2183
    • (2006) J. Cell Sci. , vol.119 , pp. 2173-2183
    • Appenzeller-Herzog, C.1    Hauri, H.P.2
  • 13
    • 0037013292 scopus 로고    scopus 로고
    • Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum
    • Velloso L.M., Svensson K., Schneider G., Pettersson R.F., and Lindqvist Y. Crystal structure of the carbohydrate recognition domain of p58/ERGIC-53, a protein involved in glycoprotein export from the endoplasmic reticulum. J. Biol. Chem. 277 (2002) 15979-15984
    • (2002) J. Biol. Chem. , vol.277 , pp. 15979-15984
    • Velloso, L.M.1    Svensson, K.2    Schneider, G.3    Pettersson, R.F.4    Lindqvist, Y.5
  • 14
    • 0344873595 scopus 로고    scopus 로고
    • The crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding
    • Velloso L.M., Svensson K., Pettersson R.F., and Lindqvist Y. The crystal structure of the carbohydrate-recognition domain of the glycoprotein sorting receptor p58/ERGIC-53 reveals an unpredicted metal-binding site and conformational changes associated with calcium ion binding. J. Mol. Biol. 334 (2003) 845-851
    • (2003) J. Mol. Biol. , vol.334 , pp. 845-851
    • Velloso, L.M.1    Svensson, K.2    Pettersson, R.F.3    Lindqvist, Y.4
  • 16
    • 38949176056 scopus 로고    scopus 로고
    • Deletion of 3 residues from the C-terminus of MCFD2 affects binding to ERGIC-53 and causes combined factor V and factor VIII deficiency
    • Nyfeler B., Kamiyaa Y., Boehlen F., Yamamoto K., Kato K., de Moerloose P., Hauri H.P., and Neerman-Arbez M. Deletion of 3 residues from the C-terminus of MCFD2 affects binding to ERGIC-53 and causes combined factor V and factor VIII deficiency. Blood 111 (2008) 1299-1301
    • (2008) Blood , vol.111 , pp. 1299-1301
    • Nyfeler, B.1    Kamiyaa, Y.2    Boehlen, F.3    Yamamoto, K.4    Kato, K.5    de Moerloose, P.6    Hauri, H.P.7    Neerman-Arbez, M.8
  • 17
    • 58149140521 scopus 로고    scopus 로고
    • The first case of combined coagulation factor V and coagulation factor VIII deficiency in Poland due to a novel p.Tyr135Asn missense mutation in the MCFD2 gene
    • Ivaskevicius V., Windyga J., Baran B., Bykowska K., Daugela L., Watzka M., Seifried E., and Oldenburg J. The first case of combined coagulation factor V and coagulation factor VIII deficiency in Poland due to a novel p.Tyr135Asn missense mutation in the MCFD2 gene. Blood Coagul. Fibrinolysis 19 (2008) 531-534
    • (2008) Blood Coagul. Fibrinolysis , vol.19 , pp. 531-534
    • Ivaskevicius, V.1    Windyga, J.2    Baran, B.3    Bykowska, K.4    Daugela, L.5    Watzka, M.6    Seifried, E.7    Oldenburg, J.8
  • 18
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41 (2005) 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 19
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26 (1993) 795-800
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 20
    • 0028103275 scopus 로고    scopus 로고
    • Collaborative Computational Project, Number 4. (1994). The CCP4 Suite: Programs for Protein Crystallography. Acta Cryst. D 50, 760-763.
    • Collaborative Computational Project, Number 4. (1994). The CCP4 Suite: Programs for Protein Crystallography. Acta Cryst. D 50, 760-763.
  • 23
    • 77949535720 scopus 로고    scopus 로고
    • Emsley, P. Lohkamp, B., Scott W.G. and Cowtan, K. (2010) Features and Development of Coot. Acta Cryst. D 66 (in press).
    • Emsley, P. Lohkamp, B., Scott W.G. and Cowtan, K. (2010) Features and Development of Coot. Acta Cryst. D 66 (in press).
  • 24
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov G.N., Vagin A.A., and Dodson E.J. Refinement of macromolecular structures by the maximum-likelihood method. Acta Cryst. D 53 (1997) 240-255
    • (1997) Acta Cryst. D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 25
    • 76749102606 scopus 로고    scopus 로고
    • DeLano Scientific, San Carlos, CA
    • W.L. DeLano, The PyMOL Molecular Graphics System, DeLano Scientific, San Carlos, CA (2002) http://www.pymol.org.
    • (2002)
    • DeLano, W.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.