Human α2-macroglobulin is composed of multiple domains, as predicted by homology with complement component C3

Biochemical Journal

Volumn 407, Issue 1, 2007, Pages 23-30

  Doan, Ninh ^a   Gehins, Peter G W ^a  

^a UNIVERSITY OF ILLINOIS AT CHICAGO   (United States)

Author keywords

2 macroglobulin ( 2M); Complement component C3; Crystal structure; Domain organization; Receptor binding domain; Thiol ester

Indexed keywords

ACTIVATION ANALYSIS; ESTERS; GENE EXPRESSION; MOLECULAR STRUCTURE; PROTEOLYSIS;

COMPLEMENT COMPONENT C3; DOMAIN ORGANIZATION; RECEPTOR-BINDING DOMAIN; THIOL ESTERS;

PROTEINS;

ALPHA 2 MACROGLOBULIN; COMPLEMENT COMPONENT C3; FIBRONECTIN; GROWTH FACTOR; PROCOLLAGEN C PROTEINASE; THIOESTER; COMPLEMENTARY DNA; ESTER;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DNA FLANKING REGION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN EXPRESSION; PROTEIN FOLDING; PROTEIN PURIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; SEQUENCE HOMOLOGY; X RAY CRYSTALLOGRAPHY; BINDING SITE; BIOLOGICAL MODEL; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PROTEIN TERTIARY STRUCTURE; STRUCTURAL HOMOLOGY; STRUCTURE ACTIVITY RELATION; TEMPERATURE;

ALPHA-MACROGLOBULINS; BINDING SITES; COMPLEMENT C3; DNA, COMPLEMENTARY; ESTERS; HUMANS; MODELS, BIOLOGICAL; MODELS, MOLECULAR; PROTEIN STRUCTURE, TERTIARY; STRUCTURAL HOMOLOGY, PROTEIN; STRUCTURE-ACTIVITY RELATIONSHIP; TEMPERATURE;

EID: 35148893714     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20070764     Document Type: Article

References (34)

1. Sottrup-Jensen, L. (1989) α-Macroglobulins. Structure, shape, and mechanism of proteinase complex formation. J. Biol. Chem. 264, 11539-11542
2. 2-macroglobulin with proteinases. Characteristics and specificity of the reaction and a hypothesis concerning its molecular mechanism. Biochem. J. 133, 709-724
3. 2-macroglobulin. Arch. Biochem. Biophys. 292, 487-492
4. 2-macroglobulin. Biochem. Biophys. Res. Commun. 87, 330-336
5. 2-macroglobulin and effects of proteases and methylamine. Biochemistry 25, 5011-5017
6. 2-macroglobulin. FEBS Lett. 127, 167-173
7. Sottrup-Jensen, L., Sand, O., Kristensen, L. and Fey, G. H. (1989) The α-macroglobulin bait region. Sequence diversity and localization of cleavage sites for proteinases in five mammalian α-macroglobulins. J. Biol. Chem. 264, 15781-15789
8. 2-macroglobulin. Characterization of a receptor-binding domain obtained by digestion with papain. FEBS Lett. 205, 20-24
9. 2M) that can react rapidly to incorporate not only methylamine or putrescine but also proteins lacking proteinase activity. FEBS Lett. 128, 123-126
10. 2-macroglobulin during activation with trypsin. Biochem. Biophys. Res. Commun. 107, 93-100
11. 2- macroglobulin receptor. FEBS Lett. 276, 151-155
12. Bacskai, B. J., Xia, M. Q., Strickland, D. K., Rebeck, G. W. and Hyman, B. T. (2000) The endocytic receptor protein LRP also mediates neuronal calcium signaling via N-methyl-D-aspartate receptors. Proc. Natl. Acad. Sci. U.S.A. 97, 11551-11556
13. 2-macroglobulin and complement components C3 and C4. Proc. Natl. Acad. Sci. U.S.A. 82, 9-13
14. Wiesmann, C., Katschke, Jr, K. J., Yin, J. P., Helmy, K. Y., Steffek, M., Fairbrother, W. J., McCallum, S. A., Embuscado, L., DeForge, L., Hass, P. E. and van Lookeren Campagne, M. (2006) Structure of C3b in complex with CRIg gives insights into regulation of complement activation. Nature 444, 217-220
15. Janssen, B. J. C., Christodouliou, A., McCarthy, A., Lambris, J. D. and Gros, P. (2006) Structure of C3b reveals conformational changes that underlie complement activity. Nature 444, 213-216
16. Ajees, A., Gunasekaran, K., Narayana, S. V. L., Kotwal, G. J. and Murthy, H. M. K. (2006) The structure of complement C3b provides insights into complement activation and regulation. Nature 444, 221-225
17. Janssen, B. J. C., Huizinga, E. G., Raaijmakers, H. C. A., Roos, A., Daha, M. R., Nilsson-Ekdahl, K., Nilsson, B. and Gros, P. (2005) Structures of complement component C3 provide insights into the function and evolution of immunity. Nature 437, 505-511
18. 2- macroglobulin. Protein Sci. 7, 2602-2612
19. 2- macroglobulin. Isolation after limited proteolysis with a bacterial proteinase. J. Biol. Chem. 261, 11369-11373
20. 2- macroglobulin. Structure 6, 595-604
21. Huang, W., Dolmer, K., Liao, X. and Gettins, P. G. W. (2000) NMR solution structure of the receptor binding domain of human α2macroglobulin. J. Biol. Chem. 275, 1089-1094
22. Nagar, B., Jones, R. G., Diefenbach, R. J., Isenman, D. E. and Rini, J. M. (1998) X-ray crystal structure of C3d: A C3 fragment and ligand for complement receptor 2. Science 280, 1277-1281
23. van den Elsen, J. M. H., Martin, A., Wong, V., Clemenza, L., Rose, D. R. and Isenman, D. E. (2002) X-ray crystal structure of the C4d fragment of human complement component C4. J. Mol. Biol. 322, 1103-1115
24. Yang, J. T., Wu, C.-S. C. and Martinez, H. M. (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol. 130, 208-269
25. Chang, C. T., Wu, C.-S. C. and Yang, J. T. (1978) Circular dichroic analysis of protein conformation: inclusion of the β-turns. Anal. Biochem. 91, 13-31
26. Privalov, P. L. (1982) Stability of proteins. Proteins which do not present a single cooperative system. Adv. Protein Chem. 35, 1-104
27. Ellman, G. L. (1959) Tissue sulfhydryl groups. Arch. Biochem. Biophys. 82, 70-77
28. 2-macroglobulin half-molecules induced by cadmium. Biochem. Biophys. Res. Commun. 149, 488-492
29. 2-macroglobulin into functional half-molecules by mild acid treatment. Biochim. Biophys. Acta 996, 132-138
30. 2-macroglobulin and pregnancy zone protein. Eur. J. Biochem. 210, 1071-1077
31. 2Macroglobulin variants. A role for the bait region in tetramer formation. J. Biol. Chem. 270, 14160-14167
32. Bork, P. and Beckmann, G. (1993) The CUB domain: a widespread module in developmentally regulated proteins. J. Mol. Biol. 231, 539-545
33. 2-macroglobulin. Complete disulfide bridge assignment and localization of two intrachain bridges in the dimeric proteinase binding unit. J. Biol. Chem. 261, 15863-15869
34. Oxvig, C., Gleich, G. J. and Sottrup-Jensen, L. (1994) Localization of disulfide bridges and free sulfhydryl groups in human eosinophil granule major basic protein. FEBS Lett. 341, 213-217