ArticleThe Journal of biological chemistry2017
Structural analyses of von Willebrand factor C domains of collagen 2A and CCN3 reveal an alternative mode of binding to bone morphogenetic protein-2.
Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 33 citations in OpenAlex.
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- Structural insights into regulation of CCN protein activities and functions.Journal of cell communication and signaling · 2023Review
- The carboxyl-terminal TSP1-homology domain is the biologically active effector peptide of matricellular protein CCN5 that counteracts profibrotic CCN2.The Journal of biological chemistry · 2023Article
- Modelling the structure of Short Gastrulation and generation of a toolkit for studying its function in Drosophila.Biology open · 2022Article
- Expanding the clinical spectrum of COL2A1 related disorders by a mass like phenotype.Scientific reports · 2022Article
- SCO-spondin, a giant matricellular protein that regulates cerebrospinal fluid activity.Fluids and barriers of the CNS · 2021Review
- lncRNAOncology letters · 2021Article
- Collagen Biosynthesis, Processing, and Maturation in Lung Ageing.Frontiers in medicine · 2021Review
- Review
- Connective Tissue Growth Factor: From Molecular Understandings to Drug Discovery.Frontiers in cell and developmental biology · 2020Review
- Structural biology of the TGFβ family.Experimental biology and medicine (Maywood, N.J.) · 2019Review
- Acquired Von Willebrand Syndrome (AVWS) in cardiovascular disease: a state of the art review for clinicians.Journal of thrombosis and thrombolysis · 2019Review
- Structure and dynamics of the platelet integrin-binding C4 domain of von Willebrand factor.Blood · 2019Article
- Connective tissue growth factor (CCN2) is a matricellular preproprotein controlled by proteolytic activation.The Journal of biological chemistry · 2018Article
- The concept of the CCN protein family revisited: a centralized coordination network.Journal of cell communication and signaling · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bone morphogenetic proteins (BMPs) are secreted growth factors that promote differentiation processes in embryogenesis and tissue development. Regulation of BMP signaling involves binding to a variety of extracellular proteins, among which are many von Willebrand factor C (vWC) domain-containing proteins. Although the crystal structure of the complex of crossveinless-2 (CV-2) vWC1 and BMP-2 previously revealed one mode of the vWC/BMP-binding mechanism, other vWC domains may bind to BMP differently. Here, using X-ray crystallography, we present for the first time structures of the vWC domains of two proteins thought to interact with BMP-2: collagen IIA and matricellular protein CCN3. We found that these two vWC domains share a similar N-terminal fold that differs greatly from that in CV-2 vWC, which comprises its BMP-2-binding site. We analyzed the ability of these vWC domains to directly bind to BMP-2 and detected an interaction only between the collagen IIa vWC and BMP-2. Guided by the collagen IIa vWC domain crystal structure and conservation of surface residues among orthologous domains, we mapped the BMP-binding epitope on the subdomain 1 of the vWC domain. This binding site is different from that previously observed in the complex between CV-2 vWC and BMP-2, revealing an alternative mode of interaction between vWC domains and BMPs.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.