Unraveling the Mechanism of Procollagen C-Proteinase Enhancer

Michael P Lockhart-Cairns; Clair Baldock

doi:10.1016/j.str.2018.09.003

Unraveling the Mechanism of Procollagen C-Proteinase Enhancer

Structure. 2018 Oct 2;26(10):1299-1301. doi: 10.1016/j.str.2018.09.003.

Authors

Michael P Lockhart-Cairns¹, Clair Baldock²

Affiliations

¹ Wellcome Centre for Cell-Matrix Research, Division of Cell-Matrix Biology and Regenerative Medicine, School of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK.
² Wellcome Centre for Cell-Matrix Research, Division of Cell-Matrix Biology and Regenerative Medicine, School of Biological Sciences, Faculty of Biology, Medicine and Health, University of Manchester, Manchester Academic Health Science Centre, Manchester, UK. Electronic address: clair.baldock@manchester.ac.uk.

PMID: 30282017
DOI: 10.1016/j.str.2018.09.003

Abstract

In this issue of Structure, Pulido et al. (2018) determine the crystal structure of procollagen C-proteinase enhancer-1 (PCPE-1)/procollagen III complex and identify that PCPE-1 unwinds the stalk of the procollagen III trimer, liberating a single chain to facilitate binding and cleavage by BMP-1 proteinases for subsequent fibrillar collagen assembly.

Publication types

Research Support, Non-U.S. Gov't
Comment

MeSH terms

Bone Morphogenetic Protein 1
Extracellular Matrix Proteins*
Glycoproteins
Procollagen*

Substances

Extracellular Matrix Proteins
Glycoproteins
Procollagen
Bone Morphogenetic Protein 1

Abstract

Publication types

MeSH terms

Substances

Grants and funding