1lre Citations

The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein.

Proc. Natl. Acad. Sci. U.S.A. 94 7521-5 (1997)
Cited: 30 times
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Abstract

The three-dimensional structure of the N-terminal domain (residues 18-112) of alpha2-macroglobulin receptor-associated protein (RAP) has been determined by NMR spectroscopy. The structure consists of three helices composed of residues 23-34, 39-65, and 73-88. The three helices are arranged in an up-down-up antiparallel topology. The C-terminal 20 residues were shown not to be in a well defined conformation. A structural model for the binding of RAP to the family of low-density lipoprotein receptors is proposed. It defines a role in binding for both the unordered C terminus and the structural scaffold of the core structure. Pathogenic epitopes for the rat disease Heymann nephritis, an experimental model of human membranous glomerulonephritis, have been identified in RAP and in the large endocytic receptor gp330/megalin. Here we provide the three-dimensional structure of the pathogenic epitope in RAP. The amino acid residues known to form the epitope are in a helix-loop-helix conformation, and from the structure it is possible to rationalize the published results obtained from studies of fragments of the N-terminal domain.

Articles - 1lre mentioned but not cited (5)

  1. Fold prediction of helical proteins using torsion angle dynamics and predicted restraints. Zhang C, Hou J, Kim SH. Proc. Natl. Acad. Sci. U.S.A. 99 3581-3585 (2002)
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  3. The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein. Nielsen PR, Ellgaard L, Etzerodt M, Thogersen HC, Poulsen FM. Proc. Natl. Acad. Sci. U.S.A. 94 7521-7525 (1997)
  4. Structure prediction for the helical skeletons detected from the low resolution protein density map. Al Nasr K, Sun W, He J. BMC Bioinformatics 11 Suppl 1 S44 (2010)
  5. Reduction of the secondary structure topological space through direct estimation of the contact energy formed by the secondary structures. Sun W, He J. BMC Bioinformatics 10 Suppl 1 S40 (2009)


Reviews citing this publication (5)

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Articles citing this publication (20)

  1. Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors. Fisher C, Beglova N, Blacklow SC. Mol. Cell 22 277-283 (2006)
  2. Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif. Jensen GA, Andersen OM, Bonvin AM, Bjerrum-Bohr I, Etzerodt M, Thøgersen HC, O'Shea C, Poulsen FM, Kragelund BB. J. Mol. Biol. 362 700-716 (2006)
  3. Clean TROSY: compensation for relaxation-induced artifacts. Schulte-Herbrüggen T, Sorensen OW. J. Magn. Reson. 144 123-128 (2000)
  4. RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi. Lee D, Lee D, Walsh JD, Mikhailenko I, Yu P, Migliorini M, Wu Y, Krueger S, Curtis JE, Harris B, Lockett S, Blacklow SC, Strickland DK, Wang YX. Mol. Cell 22 423-430 (2006)
  5. Receptor-associated protein interacts with amyloid-beta peptide and promotes its cellular uptake. Kanekiyo T, Bu G. J. Biol. Chem. 284 33352-33359 (2009)
  6. Crystal structure of the receptor-binding domain of alpha 2-macroglobulin. Jenner L, Husted L, Thirup S, Sottrup-Jensen L, Nyborg J. Structure 6 595-604 (1998)
  7. The role of coherence transfer efficiency in design of TROSY-type multidimensional NMR experiments. Meissner A, Sørensen OW. J. Magn. Reson. 139 439-442 (1999)
  8. The carboxy-terminal domain of the receptor-associated protein binds to the Vps10p domain of sortilin. Tauris J, Ellgaard L, Jacobsen C, Nielsen MS, Madsen P, Thøgersen HC, Gliemann J, Petersen CM, Moestrup SK. FEBS Lett. 429 27-30 (1998)
  9. The structure of receptor-associated protein (RAP). Lee D, Lee D, Walsh JD, Migliorini M, Yu P, Cai T, Schwieters CD, Krueger S, Strickland DK, Wang YX. Protein Sci. 16 1628-1640 (2007)
  10. DNA vaccination against specific pathogenic TCRs reduces proteinuria in active Heymann nephritis by inducing specific autoantibodies. Wu H, Walters G, Knight JF, Alexander SI. J Immunol 171 4824-4829 (2003)
  11. Optimization of three-dimensional TROSY-type HCCH NMR correlation of aromatic (1)H-(13)C groups in proteins. Meissner A, Sorensen OW. J. Magn. Reson. 139 447-450 (1999)
  12. Three-dimensional protein NMR TROSY-type (15)N-resolved (1)H(N)-(1)H(N) NOESY spectra with diagonal peak suppression. Meissner A, SŁrensen OW. J. Magn. Reson. 142 195-198 (2000)
  13. Infiltration of canonical Vgamma4/Vdelta1 gammadelta T cells in an adriamycin-induced progressive renal failure model. Ando T, Wu H, Watson D, Hirano T, Hirakata H, Fujishima M, Knight JF. J Immunol 167 3740-3745 (2001)
  14. Dissection of RAP-LRP interactions: binding of RAP and RAP fragments to complement-like repeats 7 and 8 from ligand binding cluster II of LRP. Lazic A, Dolmer K, Strickland DK, Gettins PG. Arch. Biochem. Biophys. 450 167-175 (2006)
  15. Editing of multidimensional NMR spectra of partially deuterated proteins. Measurement of amide deuterium isotope effects on the chemical shifts of protein backbone nuclei. Meissner A, Briand J, Sφrensen OW. J. Biomol. NMR 12 339-343 (1998)
  16. NMR structural studies of domain 1 of receptor-associated protein. Wu Y, Migliorini M, Walsh J, Yu P, Strickland DK, Wang YX. J. Biomol. NMR 29 271-279 (2004)
  17. New multidimensional editing experiments for measurement of amide deuterium isotope effects on Cbeta chemical shifts in 13C, 15N-labeled proteins. Meissner A, Sørensen OW. J. Magn. Reson. 135 547-550 (1998)
  18. Suppression of diagonal peaks in three-dimensional protein NMR TROSY-type HCCH correlation experiments. Meissner A, Sorensen OW. J. Magn. Reson. 144 171-174 (2000)
  19. High Affinity Binding of the Receptor-associated Protein D1D2 Domains with the Low Density Lipoprotein Receptor-related Protein (LRP1) Involves Bivalent Complex Formation: CRITICAL ROLES OF LYSINES 60 AND 191. Prasad JM, Young PA, Strickland DK. J. Biol. Chem. 291 18430-18439 (2016)
  20. T cell lines specific for a synthetic Heymann nephritis peptide derived from the receptor-associated protein. Wu H, Zhang GY, Knight JF. Clin. Exp. Immunol. 121 157-164 (2000)


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