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Related Experiment Video

Updated: Jul 8, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

Published on: June 3, 2014

Structures of thrombospondins.

C B Carlson¹, J Lawler, D F Mosher

¹Department of Biomolecular Chemistry, University of Wisconsin, Madison, Wisconsin 53706, USA.

Cellular and Molecular Life Sciences : CMLS

|January 15, 2008

Summary

This summary is machine-generated.

High-resolution structures of thrombospondins, large secreted glycoproteins, reveal unique motifs. Combining structural data allows modeling thrombospondin-1 and -2, offering insights into their cellular functions.

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Last Updated: Jul 8, 2026

Helical Organization of Blood Coagulation Factor VIII on Lipid Nanotubes

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Area of Science:

Biochemistry
Structural Biology
Cellular Biology

Background:

Thrombospondins are large, secreted, multimodular, calcium-binding glycoproteins.
They play complex roles in mediating various cellular processes.

Purpose of the Study:

To review progress in determining high-resolution structures of thrombospondins.
To discuss the functional implications of these structural findings.

Main Methods:

Analysis of high-resolution structures of thrombospondin modules.
Integration of structural data from thrombospondins and related extracellular proteins.

Main Results:

Identification of unique and interesting protein motifs within thrombospondins.
Development of an overall structural model for thrombospondin-1 and thrombospondin-2.
Discernment of structural features in other thrombospondins.

Conclusions:

High-resolution structural determination provides critical insights into thrombospondin function.
Integrated structural models enhance understanding of thrombospondin family members.