Collagen stabilization at atomic level: Crystal structure of designed (GlyProPro)10foldon

Structure

Volumn 11, Issue 3, 2003, Pages 339-346

  Stetefeld, Jörg ^a   Frank, Sabine ^a   Jenny, Margrit ^a   Schulthess, Therese ^a   Kammerer, Richard A ^a,c   Boudko, Sergei ^a   Landwehr, Ruth ^a   Okuyama, Kenji ^b   Engel, Jürgen ^a  

^a UNIVERSITY OF BASEL   (Switzerland)

^b TOKYO UNIVERSITY OF AGRICULTURE AND TECHNOLOGY   (Japan)

^c UNIVERSITY OF MANCHESTER   (United Kingdom)

Author keywords

Collagen folding; Collagen stability; Foldon; Hetero assembly; NC domain; Protein design

Indexed keywords

GLYCYLPROLYLPROLINE; HYBRID PROTEIN; PEPTIDE; UNCLASSIFIED DRUG; VIRUS PROTEIN;

ARTICLE; BACTERIOPHAGE T4; CARBOXY TERMINAL SEQUENCE; CRYSTAL STRUCTURE; ENTROPY; MELTING POINT; MOLECULAR BIOLOGY; OPTICAL RESOLUTION; PRIORITY JOURNAL; PROTEIN ISOLATION; PROTEIN STABILITY; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TRIPLE HELIX;

ANIMALS; COLLAGEN; CRYSTALLOGRAPHY, X-RAY; HUMANS; PEPTIDES; PROTEIN ENGINEERING; PROTEIN STRUCTURE, TERTIARY;

EID: 0037337514     PISSN: 09692126     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0969-2126(03)00025-X     Document Type: Article

References (38)

1. Bateman J.F., Lamande S.R., Ramshaw J.A.M. Collagen superfamily. Comper W.D. Extracellular Matrix, Volume 2. 1996;Harwood Academic Publishers, Amsterdam. 22-67.pp.
2. Traub W., Piez K.A. The chemistry and structure of collagen. Adv. Protein Chem. 25:1971;243-352.
3. Hakansson K., Reid K.B. Collectin structure. a review Protein Sci. 9:2000;1607-1617.
4. Brodsky B. Hydrogen bonding in the triple-helix. Proc. Indian Acad. Sci. 111:1999;13-18.
5. Crick F.H.C., Rich A. The molecular structure of collagen. Nature. 176:1955;780.
6. Ramachandran G.N., Kartha G. Structure of collagen. Nature. 176:1955;593-595.
7. Engel J., Chen H.T., Prockop D.J., Klump H. The triple helix in equilibrium with coil conversion of collagen-like polytripeptides in aqueous and nonaqueous solvents. Comparison of the thermodynamic parameters and the binding of water to (L-Pro-L-Pro-Gly)n and (L-Pro-L-Hyp-Gly)n. Biopolymers. 16:1977;601-622.
8. Okuyama K., Nagarajan V., Kamitori S. 7/2-helical model for collagen - evidence from model peptides. Proc. Indian Acad. Sci. 111:1999;19-34.
9. Kramer R.Z., Vitagliano L., Bella J., Berisio R., Mazzarella L., Brodsky B., Zagari A., Berman H.M. X-ray crystallographic determination of a collagen-like peptide with the repeating sequence (Pro-Pro-Gly). J. Mol. Biol. 280:1998;623-638.
10. Holmgren S.K., Taylor K.M., Bretscher L.E., Raines R.T. Code for collagen's stability deciphered. Nature. 392:1998;666-667.
11. Jenkins C.L., Raines R.T. Insights on the conformational stability of collagen. Nat. Prod. Rep. 19:2002;49-59.
12. Sundaramoorthy M., Meiyappan M., Todd P., Hudson B.G. Crystal structure of NC1 domains. structural basis for type IV collagen assembly in basement membranes J. Biol. Chem. 277:2002;31142-31153.
13. Than M.E., Henrich S., Huber R., Ries A., Mann K., Kuhn K., Timpl R., Bourenkov G.P., Bartunik H.D., Bode W. The 1.9 Å crystal structure of the noncollagenous (NC1) domain of human placenta collagen IV shows stabilization via a novel type of covalent Met-Lys cross-link. Proc. Natl. Acad. Sci. USA. 99:2002;6607-6612.
14. Bogin O., Kvansakul M., Rom E., Singer J., Yayon A., Hohenester E. Insight into Schmid metaphyseal chondrodysplasia from the crystal structure of the collagen X NC1 domain trimer. Structure. 10:2002;165-173.
15. Lesage A., Penin F., Geourjon C., Marion D., van der Rest M. Trimeric assembly and three-dimensional structure model of the FACIT collagen COL1-NC1 junction from CD and NMR analysis. Biochemistry. 35:1996;9647-9660.
16. Snellman A., Tu H., Vaisanen T., Kvist A.P., Huhtala P., Pihlajaniemi T. A short sequence in the N-terminal region is required for the trimerization of type XIII collagen and is conserved in other collagenous transmembrane proteins. EMBO J. 19:2000;5051-5059.
17. Bächinger H.P., Bruckner P., Timp R., Prockop D.J., Engel J. Folding mechanism of the triple helix in type-III collagen and type-III pN-collagen. Role of disulfide bridges and peptide bond isomerization. Eur. J. Biochem. 106:1980;619-632.
18. Bruckner P., Bächinger H.P., Timpl R., Engel J. Three conformationally distinct domains in the amino-terminal segment of type III procollagen and its rapid triple helix leads to and comes from coil transition. Eur. J. Biochem. 90:1978;595-603.
19. Dölz R., Engel J., Kühn K. Folding of collagen IV. Eur. J. Biochem. 178:1988;357-366.
20. Hoppe H.J., Barlow P.N., Reid K.B. A parallel three stranded alpha-helical bundle at the nucleation site of collagen triple-helix formation. FEBS Lett. 344:1994;191-195.
21. Boudko S., Frank S., Kammerer R.A., Stetefeld J., Schulthess T., Landwehr R., Lustig A., Bachinger H.P., Engel J. Nucleation and propagation of the collagen triple helix in single-chain and trimerized peptides. transition from third to first order kinetics J. Mol. Biol. 317:2002;459-470.
22. Engel J., Kammerer R.A. What are oligomerization domains good for? Matrix Biol. 19:2000;283-288.
23. Frank S., Kammerer R.A., Mechling D., Schulthess T., Landwehr R., Bann J., Guo Y., Lustig A., Bachinger H.P., Engel J. Stabilization of short collagen-like triple helices by protein engineering. J. Mol. Biol. 308:2001;1081-1089.
24. Brass A., Kadler K.E., Thomas J.T., Grant M.E., Boot-Handford R.P. The fibrillar collagens, collagen VIII, collagen X and the C1q complement proteins share a similar domain in their C-terminal non-collagenous regions. FEBS Lett. 303:1992;126-128.
25. Letarov A.V., Londer Y.Y., Boudko S., Mesyanzhinov V.V. The carboxy-terminal domain initiates trimerization of bacteriophage T4 fibritin. Biochemistry. 64:1999;817-823.
26. Strelkov S.V., Tao Y., Shneider M., Mesyanzhinov V.V., Rossmann M.G. Structure of bacteriophage T4 fibritin M. a troublesome packing arrangement Acta Crystallogr. D Biol. Crystallogr. 54:1998;805-816.
27. Okuyama K., Okuyama K., Arnott S., Takayanagi M., Kakudo M. Crystal and molecular structure of a collagen-like polypeptide (Pro-Pro- Gly)10. J. Mol. Biol. 152:1981;427-443.
28. Berisio R., Vitagliano L., Mazzarella L., Zagari A. Crystal structure of the collagen triple helix model. Protein Sci. 11:2002;262-270.
29. Bella J., Eaton M., Brodsky B., Berman H.M. Crystal and molecular structure of a collagen-like peptide at 1.9 Å resolution. Science. 266:1994;75-81.
30. Bella J., Brodsky B., Berman H.M. Hydration structure of a collagen peptide. Structure. 3:1995;893-906.
31. Tao Y., Strelkov S., Mesyanzhinov V.V., Rossmann M.G. Structure of bacteriophage T4 fibritin. a segmented coiled coil and the role of the C-terminal domain Structure. 5:1997;789-798.
32. Timpl R., Wiedemann H., van Deleden V., Furthmayr H., Kühn K. A network model for the organization of type IV collagen molecules in basement mebranes. Eur. J. Biochem. 120:1981;203-211.
33. Yurchenco P., Furthmayr H. Self-assembly of basement membrane collagen. Biochemistry. 23:1984;1839-1850.
34. Leslie A.G.W. MOSFLM Users Guide. 1994;Cambridge, MRC-LMB.
35. The CCP4 suite. programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50:1994;760-763.
36. Brunger A.T., Adams P.D., Clore G.M., DeLano W.L., Gros P., Grosse-Kunstleve R.W., Jiang J.S., Kuszewski J., Nilges M., Pannu N.S.et al. Crystallography and NMR system. a new software suite for macromolecular structure determination Acta Crystallogr. D Biol. Crystallogr. 54:1998;905-921.
37. Turk, D.C. (1992). Weiterentwicklung eines programmes für molekülgraphik und elektronendichte-manipulation und seine anwendung auf verschiedene protein-strukturaufklärungen. PhD thesis, Technische Universität München, Munich, Germany.
38. Engh R.A., Huber R. Accurate bond and angle parameters for X-ray protein structure refinement. Acta Crystallogr. A. 47:1991;392-400.