Order out of complexity--protein structures that interact with heparin
Related Experiment Video
Updated: Oct 3, 2026

Using a GFP-tagged TMEM184A Construct for Confirmation of Heparin Receptor Identity
Published on: February 17, 2017
1Laboratory for Molecular Structure, National Institute for Biological Standards and Control, Hertfordshire, UK. bmulloy@nibsc.ac.uk
Abstract:
Many proteins of widely differing functionality and structure are capable of binding heparin. Structural characterisations of the many types of such complexes are being reported in ever-increasing number and at improved resolution. Several crystal structures of complexes formed through the interaction of heparin-derived oligosaccharides with one or more protein partners have been described.
Related Concept Videos
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complex Assembly
Many viruses self-assemble into a fully functional unit using the infected host cell to...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Protein Complexes with Interchangeable Parts
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Anticoagulant Drugs: Low-Molecular-Weight Heparins
Protein-protein Interfaces
