The Crystal Structure of the Collagen-like Polypeptide (Glycyl-4(R)-hydroxyprolyl-4(R)-hydroxyprolyl)9 at 1.55 Å Resolution Shows Up-puckering of the Proline Ring in the Xaa Position
Open Access
- 1 May 2005
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 280 (21), 20397-20403
- https://doi.org/10.1074/jbc.m501453200
Abstract
No abstract availableKeywords
This publication has 47 references indexed in Scilit:
- Collagens, modifying enzymes and their mutations in humans, flies and wormsTrends in Genetics, 2004
- Crystal structures of collagen model peptides with Pro‐Hyp‐Gly repeating sequence at 1.26 Å resolution: Implications for proline ring puckeringPeptide Science, 2004
- Prolyl 4-hydroxylases, the key enzymes of collagen biosynthesisMatrix Biology, 2003
- Crystal structure of the collagen triple helix model [(Pro‐Pro‐Gly)10]3Protein Science, 2002
- Collagen biosynthesis: A mini-review clusterMatrix Biology, 1998
- Glycosylated Threonine but not 4-Hydroxyproline Dominates the Triple Helix Stabilizing Positions in the Sequence of a Hydrothermal Vent Worm Cuticle CollagenJournal of Molecular Biology, 1996
- Perspectives on the synthesis and application of triple-helical, collagen-model peptidesBiopolymers, 1996
- NMR and x-ray studies of collagen model peptidesBiopolymers, 1996
- Structural Comparison of Cuticle and Interstitial Collagens from Annelids Living in Shallow Sea-water and at Deep-sea Hydrothermal VentsJournal of Molecular Biology, 1995
- Synthesis and investigation of collagen model peptidesPublished by Springer Nature ,1982