ColBuilder: a server to build collagen fibril models
Type I collagen is the main structural component of many tissues in the human body. It provides excellent mechanical properties to connective tissue and acts as a protein interaction hub. There is thus a wide interest in understanding the properties and diverse functions of type I collagen at the mo...
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| Main Authors: | , , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
13 July 2021
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| In: |
Biophysical journal
Year: 2021, Volume: 120, Issue: 17, Pages: 3544-3549 |
| ISSN: | 1542-0086 |
| DOI: | 10.1016/j.bpj.2021.07.009 |
| Online Access: | Verlag, kostenfrei, Volltext: https://doi.org/10.1016/j.bpj.2021.07.009 Verlag, kostenfrei, Volltext: https://www.sciencedirect.com/science/article/pii/S0006349521005610 
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| Author Notes: | Agnieszka Obarska-Kosinska, Benedikt Rennekamp, Aysecan Ünal, and Frauke Gräter |
| Summary: | Type I collagen is the main structural component of many tissues in the human body. It provides excellent mechanical properties to connective tissue and acts as a protein interaction hub. There is thus a wide interest in understanding the properties and diverse functions of type I collagen at the molecular level. A precondition is an atomistic collagen I structure as it occurs in native tissue. To this end, we built full-atom models of cross-linked collagen fibrils by integrating the low-resolution structure of collagen fibril available from x-ray fiber diffraction with high-resolution structures of short collagen-like peptides from x-ray crystallography and mass spectrometry data. We created a Web resource of collagen models for 20 different species with a large variety of cross-link types and localization within the fibril to facilitate structure-based analyses and simulations of type I collagen in health and disease. To easily enable simulations, we provide parameters of the modeled cross-links for an Amber force field. The repository of collagen models is available at https://colbuilder.h-its.org. |
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| Item Description: | Gesehen am 10.11.2021 |
| Physical Description: | Online Resource |
| ISSN: | 1542-0086 |
| DOI: | 10.1016/j.bpj.2021.07.009 |