Structure of the haptoglobinhaemoglobin complex

Nature

Volumn 489, Issue 7416, 2012, Pages 456-459

  Andersen, Christian Brix Folsted ^a   Torvund Jensen, Morten ^a   Nielsen, Marianne Jensby ^a   De Oliveira, Cristiano Luis Pinto ^a,b   Hersleth, Hans Petter ^c   Andersen, Nielsøjmark H ^c   Pedersen, Jan Skov ^a   Andersen, Gregers Rom ^a   Moestrup, Søren Kragh ^a  

^a AARHUS UNIVERSITY   (Denmark)

^b UNIVERSITY OF SÃO PAULO   (Brazil)

^c UNIVERSITY OF OSLO   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

CD163 ANTIGEN; HAPTOGLOBIN; HEMOGLOBIN; REACTIVE OXYGEN METABOLITE; COMPLEMENT COMPONENT C1R; HEME;

BIOCHEMISTRY; BLOOD; BLOOD SYSTEM DISORDER; CHEMICAL BINDING; COMPLEXATION; CRYSTAL STRUCTURE; HEMOGLOBIN; HOMINID; LIGAND; PROTEIN; SCAVENGING (CHEMISTRY);

ALPHA HELIX; ARTICLE; BINDING AFFINITY; CELL SURFACE; DIMERIZATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CROSS LINKING; PROTEIN DOMAIN; PROTEIN INTERACTION; PROTEIN MODIFICATION; PROTEIN STRUCTURE; RADIATION SCATTERING; SWINE; ALLELE; ANIMAL; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; HUMAN; METABOLISM; NUCLEOTIDE SEQUENCE; OXIDATION REDUCTION REACTION; PROTEIN MULTIMERIZATION; PROTEIN QUATERNARY STRUCTURE; SMALL ANGLE SCATTERING; STRUCTURE ACTIVITY RELATION; X RAY DIFFRACTION;

SUS;

ALLELES; ANIMALS; BINDING SITES; COMPLEMENT C1R; CONSERVED SEQUENCE; HAPTOGLOBINS; HEME; HEMOGLOBINS; HUMANS; MODELS, MOLECULAR; OXIDATION-REDUCTION; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; SCATTERING, SMALL ANGLE; STRUCTURE-ACTIVITY RELATIONSHIP; SUS SCROFA; X-RAY DIFFRACTION;

EID: 84866504266     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature11369     Document Type: Article

References (47)

1. Bunn, H. F., Forget, B. G. & Ranney, H. M. Hemoglobinopathies 308 (W. B. Saunders Company, 1977).
2. Nagel, R. L. & Gibson, Q. H. The binding of hemoglobin to haptoglobin and its relation to subunit dissociation of hemoglobin. J. Biol. Chem. 246, 69-73 (1971).
3. Nielsen, M. J. et al. A unique loop extension in the serine protease domain of haptoglobin is essential for CD163 recognition of the haptoglobin-hemoglobin complex. J. Biol. Chem. 282, 1072-1079 (2007).
4. Kristiansen, M. et al. Identification of the haemoglobin scavenger receptor. Nature 409, 198-201 (2001).
5. Sadrzadeh, S. M., Graf, E., Panter, S. S., Hallaway, P. E. & Eaton, J. W. Hemoglobin. A biologic fenton reagent. J. Biol. Chem. 259, 14354-14356 (1984).
6. Shim, B. S., Lee, T. H. & Kang, Y. S. Immunological and biochemical investigations of human serum haptoglobin: composition of haptoglobin- haemoglobin intermediate, haemoglobin-binding sites and presence of additional alleles for b-chain. Nature 207, 1264-1267 (1965).
7. Lim, S. K. et al. Increased susceptibility in Hp knockout mice during acute hemolysis. Blood 92, 1870-1877 (1998).
8. Buehler, P. W. et al. Haptoglobin preserves the CD163 hemoglobin scavenger pathway by shielding hemoglobin from peroxidative modification. Blood 113, 2578-2586 (2009).
9. Fagoonee, S. et al. Plasma protein haptoglobinmodulates renal iron loading.Am. J. Pathol. 166, 973-983 (2005).
10. Gaboriaud, C., Rossi, V., Bally, I., Arlaud, G. J. & Fontecilla-Camps, J. C. Crystal structure of the catalytic domain of human complement C1s: a serine protease with a handle. EMBO J. 19, 1755-1765 (2000).
11. Budayova-Spano, M. et al. The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex. EMBO J. 21, 231-239 (2002).
12. Perutz, M. F. et al. Structure of haemoglobin: a three-dimensional Fourier synthesis at 5.5-A? resolution, obtained by X-ray analysis. Nature 185, 416-422 (1960).
13. Wejman, J. C., Hovsepian, D., Wall, J. S., Hainfeld, J. F. & Greer, J. Structure of haptoglobin and the haptoglobin-hemoglobin complex by electron microscopy. J. Mol. Biol. 174, 319-341 (1984).
14. Perona, J. J. & Craik, C. S. Evolutionary divergence of substrate specificity within the chymotrypsin-like serine protease fold. J. Biol. Chem. 272, 29987-29990 (1997).
15. Smulevich, G., Possenti, M., D'Avino, R., di Prisco, G. & Coletta, M. Spectroscopic studies of theheme active site ofhemoglobin fromChelidonichthys kumu. J. Raman Spectrosc. 29, 57-65 (1998).
16. Park, S.-Y., Yokoyama, T., Shibayama, N., Shiro, Y. & Tame, J. R. H. 1.25A? resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. J. Mol. Biol. 360, 690-701 (2006).
17. Kardos, J. et al. Revisiting the mechanismof the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r. Mol. Immunol. 45, 1752-1760 (2008).
18. Dickerson, R. E. & Geis, I. Hemoglobin: Structure, Function, Evolution and Pathology (The Benjamin/Cummings Publishing Company, 1983).
19. Nagel, R. L., Whittenberg, J. B. & Ranney, H. M. Oxygen Equilibria of the hemoglobin-haptoglobin complex. Biochim. Biophys. Acta 100, 286-289 (1965).
20. Venkatesh, B., Miyazaki, G., Imai, K., Morimoto, H. & Hori, H. Oxygen equilibrium and EPR studies on a1b1 hemoglobin dimer. J. Biochem. 136, 595-600 (2004).
21. Ip, S. H., Johnson, M. L. & Ackers, G. K. Kinetics of deoxyhemoglobin subunit dissociation determined by haptoglobin binding: estimation of the equilibrium constant from forward and reverse rates. Biochemistry 15, 654-660 (1976).
22. Azarov, I. et al. Rate of nitric oxide scavenging by hemoglobin bound to haptoglobin. Nitric Oxide 18, 296-302 (2008).
23. Miller, Y. I., Altamentova, S. M. & Shaklai, N. Oxidation of low-density lipoprotein by hemoglobin stems from a heme-initiated globin radical: antioxidant role of haptoglobin. Biochemistry 36, 12189-12198 (1997).
24. Pimenova, T. et al. Quantitative mass spectrometry defines an oxidative hotspot in hemoglobin that is specifically protected by haptoglobin. J. Proteome Res. 9, 4061-4070 (2010).
25. Jia, Y., Buehler, P. W., Boykins, R. A., Venable, R. M. & Alayash, A. I. Structural basis of peroxide-mediated changes in human hemoglobin: a novel oxidative pathway. J. Biol. Chem. 282, 4894-4907 (2007).
26. Smithies, O. & Walker, N. F. Notation for serum-protein groups and the genes controlling their inheritance. Nature 178, 694-695 (1956).
27. Maeda, N., Yang, F., Barnett, D. R., Bowman, B. H. & Smithies, O. Duplication within the haptoglobin Hp2 gene. Nature 309, 131-135 (1984).
28. Vanhollebeke, B. et al. A haptoglobin-hemoglobin receptor conveys innate immunity to Trypanosoma brucei in humans. Science 320, 677-681 (2008).
29. Nielsen, M. J. et al. Haptoglobin-related protein is a high-affinity hemoglobinbinding plasma protein. Blood 108, 2846-2849 (2006).
30. Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Crystallogr. 26, 795-800 (1993).
31. McCoy, A. J. et al.Phaser crystallographic software. J.Appl. Crystallogr.40, 658-674 (2007).
32. Adams, P. D. et al. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D 66, 213-221 (2010).
33. Jones, T. A., Zou, J. Y., Cowan,S. W. & Kjeldgaard, M.Improved methods for building proteinmodels in electron densitymaps and the location of errors in thesemodels. Acta Crystallogr. A 47, 110-119 (1991).
34. Krissinel, E. & Henrick, K. Inference ofmacromolecular assemblies fromcrystalline state. J. Mol. Biol. 372, 774-797 (2007).
35. Laskowski, R., MacArthur, M., Moss, D. & Thornton, J. Procheck-a program to check the stereochemical quality of protein structures. J. Appl. Crystallogr. 26, 283-291 (1993).
36. The PyMOL Molecular Graphics System v. 1.3r1 (Schro?inger, LLC, 2010).
37. Bond, C. S. & Schuettelkopf, A. W. ALINE: a WYSIWYG protein-sequence alignment editor for publication-quality alignments. Acta Crystallogr. D 65, 510-512 (2009).
38. Pedersen, J. A flux-and background-optimized version of the NanoSTAR smallangle X-ray scattering camera for solution scattering. J. Appl. Cryst. 37, 369-380 (2004).
39. Madsen, M. et al. Molecular characterization of the haptoglobin? hemoglobin receptor CD163. Ligand binding properties of the scavenger receptor cysteinerich domain region. J. Biol. Chem. 279, 51561-51567 (2004).
40. Oliveira, C. L. P. et al. A SAXS study of glucagon fibrillation. J. Mol. Biol. 387, 147-161 (2009).
41. Pedersen, J. S., Hansen, S. & Bauer, R. The aggregation behavior of zinc-free insulin studied by small-angle neutron scattering. Eur. Biophys. J. 22, 379-389 (1994).
42. Glatter, O. New method for evaluation of small-angle scattering data. J. Appl. Crystallogr. 10, 415-421 (1977).
43. Svergun, D. I. Restoring low resolution structure of biological macromolecules from solution scattering using simulated annealing. Biophys. J. 76, 2879-2886 (1999).
44. Svergun, D. I., Petoukhov, M. V. & Koch, M. H. Determination ofdomain structure of proteins from X-ray solution scattering. Biophys. J. 80, 2946-2953 (2001).
45. Svergun, D., Barberato, C. & Koch, M. CRYSOL-A program to evaluate X-ray solution scattering of biologicalmacromolecules fromatomic coordinates. J. Appl. Crystallogr. 28, 768-773 (1995).
46. Petoukhov, M. V. & Svergun, D. I. Global rigid body modeling of macromolecular complexes againstsmall-angle scattering data. Biophys. J. 89, 1237-1250 (2005).
47. Volkov, V. & Svergun, D.Uniqueness of ab initio shape determination insmall-angle scattering. J. Appl. Crystallogr. 36, 860-864 (2003).