Solution structure of 6aJL2 and 6aJL2-R24G amyloidogenics light chain proteins

Biochemical and Biophysical Research Communications

Volumn 456, Issue 2, 2015, Pages 695-699

  Maya Martinez, Roberto ^a   Gil Rodriguez, Paloma ^a   Amero, Carlos ^a  

^a CENTRO DE INVESTIGACIONES QUÍMICAS   (Mexico)

Author keywords

Amyloidosis; Immunoglobulin light chain; Nuclear Magnetic Resonance

Indexed keywords

6AJL2 PROTEIN; 6AJL2 R24G PROTEIN; AMYLOID; IMMUNOGLOBULIN LIGHT CHAIN; UNCLASSIFIED DRUG; ARGININE; GLYCINE; IMMUNOGLOBULIN LAMBDA CHAIN; SOLUTION AND SOLUBILITY;

AMYLOIDOSIS; ARTICLE; CARBON NUCLEAR MAGNETIC RESONANCE; COMPARATIVE STUDY; CRYSTAL STRUCTURE; GERM LINE; HETERONUCLEAR SINGLE QUANTUM COHERENCE; HUMAN; IN VITRO STUDY; LIGHT CHAIN; MULTIPLE ORGAN FAILURE; NITROGEN NUCLEAR MAGNETIC RESONANCE; NONHUMAN; NUCLEAR OVERHAUSER EFFECT; AMINO ACID SEQUENCE; CHEMISTRY; ENTROPY; GENETICS; METABOLISM; MOLECULAR GENETICS; POINT MUTATION; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; SOLUTION AND SOLUBILITY;

AMINO ACID SEQUENCE; AMYLOID; AMYLOIDOSIS; ARGININE; ENTROPY; GLYCINE; HUMANS; IMMUNOGLOBULIN LAMBDA-CHAINS; MOLECULAR SEQUENCE DATA; POINT MUTATION; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SOLUTIONS;

EID: 84919952336     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.12.044     Document Type: Article

References (23)

1. F. Chiti, and C.M. Dobson Protein misfolding, functional amyloid, and human disease Annu. Rev. Biochem. 75 2006 333 366 10.1146/annurev.biochem.75.101304.123901
2. V.N. Uversky, and A.L. Fink Conformational constraints for amyloid fibrillation: the importance of being unfolded Biochim. Biophys. Acta 1698 2004 131 153 10.1016/j.bbapap.2003.12.008
3. D.S. Eisenberg, and M. Jucker The amyloid state of proteins in human diseases Cell 148 2012 1188 1203 10.1016/j.cell.2012.02.022
4. M. Ramirez-Alvarado Amyloid formation in light chain amyloidosis Curr. Top. Med. Chem. 12 2012 2523 2533
5. A. Dispenzieri, M.a. Gertz, and F. Buadi What do I need to know about immunoglobulin light chain (AL) amyloidosis? Blood Rev. 26 2012 137 154 10.1016/j.blre.2012.03.001
6. G. Palladini, and R.L. Comenzo The challenge of systemic immunoglobulin light-chain amyloidosis (Al) Subcell. Biochem. 65 2012 609 642 10.1007/978-94-007-5416-4-22
7. L. del Pozo Yauner, E. Ortiz, and B. Becerril The CDR1 of the human lambdaVI light chains adopts a new canonical structure Proteins 62 2006 122 129 10.1002/prot.20779
8. L. del Pozo-Yauner, E. Ortiz, R. Sánchez, R. Sánchez-López, L. Güereca, and C.L. Murphy Influence of the germline sequence on the thermodynamic stability and fibrillogenicity of human lambda 6 light chains Proteins 72 2008 684 692 10.1002/prot.21934
9. T. Mishima, T. Ohkuri, A. Monji, T. Kanemaru, Y. Abe, and T. Ueda Residual structures in the acid-unfolded states of Vlambda6 proteins affect amyloid fibrillation J. Mol. Biol. 392 2009 1033 1043 10.1016/j.jmb.2009.07.078
10. J. Marley, M. Lu, C. Bracken, A method for efficient isotopic labeling of recombinant proteins, J. Biomol. NMR 20 (2001) 71-75. http://www.ncbi.nlm.nih.gov/pubmed/11430757.
11. E. Gasteiger, C. Hoogland, A. Gattiker, S. Duvaud, M.R. Wilkins, R.D. Appel, et al., Protein Identification and Analysis Tools on the ExPASy Server, in: J. Walker (Ed.), Humana Press, 2005.
12. L.H. Gutiérrez-González, L. Muresanu, L. del Pozo-Yauner, R. Sánchez, L. Guereca, and B. Becerril-Luján (1)H, (13)C and (15)N resonance assignment of 6aJL2(R25G), a highly fibrillogenic lambdaVI light chain variable domain Biomol. NMR Assign. 1 2007 159 161 10.1007/s12104-007-9045-9
13. F. Delaglio, S. Grzesiek, G.W. Vuister, G. Zhu, J. Pfeifer, A. Bax, NMRPipe: a multidimensional spectral processing system based on UNIX pipes, J. Biomol. NMR 6 (1995) 277-293. http://www.ncbi.nlm.nih.gov/pubmed/8520220.
14. R.L.J. Keller, The Computer Aided Resonance Assignment Tutorial, CANTINA Verlag, 2004.
15. Y. Shen, F. Delaglio, G. Cornilescu, and A. Bax TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J. Biomol. NMR 44 2009 213 223 10.1007/s10858-009-9333-z
16. C. Schwieters, J. Kuszewski, and G. Mariusclore Using Xplor-NIH for NMR molecular structure determination Prog. Nucl. Magn. Reson. Spectrosc. 48 2006 47 62 10.1016/j.pnmrs.2005.10.001
17. A. Hernández-Santoyo, L. del Pozo Yauner, D. Fuentes-Silva, E. Ortiz, E. Rudiño-Piñera, and R. Sánchez-López A single mutation at the sheet switch region results in conformational changes favoring lambda6 light-chain fibrillogenesis J. Mol. Biol. 396 2010 280 292 10.1016/j.jmb.2009.11.038
18. R. Laskowski, J.A. Rullmann, M. MacArthur, R. Kaptein, and J. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 10.1007/BF00228148
19. P.R. Pokkuluri, A. Solomon, D.T. Weiss, F.J. Stevens, M. Schiffer, Tertiary structure of human lambda 6 light chains, Amyloid 6 (1999) 165-171. http://www.ncbi.nlm.nih.gov/pubmed/10524280 (accessed 15.10.14).
20. J.S. Wall, V. Gupta, M. Wilkerson, M. Schell, R. Loris, and P. Adams Structural basis of light chain amyloidogenicity: comparison of the thermodynamic properties, fibrillogenic potential and tertiary structural features of four Vlambda6 proteins J. Mol. Recogn. 17 2004 323 331 10.1002/jmr.681
21. M. Emily, A. Talvas, and C. Delamarche MetAmyl: a METa-predictor for AMYLoid proteins PLoS One 8 2013 10.1371/journal.pone.0079722
22. C. Chothia, A.M. Lesk, Canonical structures for the hypervariable regions of immunoglobulins, J. Mol. Biol. 196 (1987) 901-917. http://www.ncbi.nlm.nih.gov/pubmed/3681981 (accessed 14.10.14).
23. W. Furey, B.C. Wang, C.S. Yoo, M. Sax, Structure of a novel Bence-Jones protein (Rhe) fragment at 1.6 Å resolution, J. Mol. Biol. 167 (1983) 661-692. http://www.ncbi.nlm.nih.gov/pubmed/6876161 (accessed 15.10.14).