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Comment on Microfibrillar structure of type I collagen in situ by Orgel et al. (2006), Proc. Natl Acad. Sci. USA, 103, 9001-9005 (Articolo in rivista)
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- Comment on Microfibrillar structure of type I collagen in situ by Orgel et al. (2006), Proc. Natl Acad. Sci. USA, 103, 9001-9005 (Articolo in rivista) (literal)
- Anno
- 2009-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1107/S0907444909023051 (literal)
- Alternative label
Okuyama K, Bächinger HP, Mizuno K, Boudko S, Engel J, Berisio R, Vitagliano L (2009)
Comment on Microfibrillar structure of type I collagen in situ by Orgel et al. (2006), Proc. Natl Acad. Sci. USA, 103, 9001-9005
in Acta crystallographica. Section D, Biological crystallography.
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- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- Okuyama K, Bächinger HP, Mizuno K, Boudko S, Engel J, Berisio R, Vitagliano L (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Okuyama, K: Department of Macromolecular Science, Graduate School of Science, Osaka University,
Toyonaka, Osaka 560-0043, Japan,
Bächinger HP, Mizuno K, Boudko S: Shriners Hospital for Children, Portland, OR 97239, USA,
Engel J, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland,
Berisio R, Vitagliano L: Istituto Biostruttre e Bioimmagini, CNR (literal)
- Titolo
- Comment on Microfibrillar structure of type I collagen in situ by Orgel et al. (2006), Proc. Natl Acad. Sci. USA, 103, 9001-9005 (literal)
- Abstract
- The molecular structure of collagen represents a long-standing issue in structural biology. The complexity and the fibrous nature of the protein prevent the application of single-crystal crystallographic techniques. Although partial information on the structure of collagen has been derived by using polypeptide models, the structural characterization of the full-length protein would provide an invaluable tool for understanding the many biological processes in which collagen is involved. The determination of the molecular structure of collagen from wide-angle X-ray fiber diffraction data has also proven to be extremely difficult, despite the progress of fiber diffraction techniques over the last eight decades. Because of a deficiency of diffraction spots on the layer lines in the wide-angle region (ca 1-30 Å resolution), it could not even be determined whether the average helical symmetry of the collagen superhelix was 7/2 (seven tripeptide units per two turns) or 10/3 (Okuyama et al., 2006[Okuyama, K., Xu, X., Iguchi, M. & Noguchi, K. (2006). Biopolymers, 84, 181-191.]). In a recently published article, Microfibrillar structure of type I collagen in situ (Orgel et al., 2006 [Orgel, J. P. R. O., Irving, T. C., Miller, A. & Wess, T. J. (2006). Proc. Natl Acad. Sci. USA, 103, 9001-9005.]), the authors report the three-dimensional molecular and packing structure of type I collagen determined by X-ray fiber diffraction analysis, which was based on 414 reflections with a completeness of 5% in the range of 5-113 Å resolution (PDB entry 1y0f ). The collagen molecule is made of three chains of more than 1000 residues each. Can we determine the three-dimensional molecular conformation based on such a small number of reflections at low resolution? Most readers would be likely to fall under this impression. However, because the fiber diffraction analysis combined with heavy-atom isomorphous replacement is a highly specialized methodology, almost all readers of Orgel's paper (including the authors of this letter initially) took their results at face value. Orgel's structure has been referenced by many researchers as the molecular structure of the collagen fibril. Furthermore, this paper was nominated as a paper of outstanding interest in recent reviews (Tsuruta & Irving, 2008[Tsuruta, H. & Irving, T. C. (2008). Curr. Opin. Struct. Biol. 18, 601-608.]; Vakonakis & Campbell, 2007[Vakonakis, I. & Campbell, I. D. (2007). Curr. Opin. Cell Biol. 19, 578-583.]).
Recently, we carefully analyzed the PDB entry 1y0f to evaluate the helical symmetry of collagen [alpha]-chains in Orgel's model. Although, as observed for most collagen-like peptides, the average helical symmetry of Orgel's model is 7/2-helix, we found some questionable aspects in their analysis. (literal)
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