Role of oligomerization domains in thrombospondins and other extracellular matrix proteins.
Coiled coils, collagen triple helices and globular oligomerization domains mediate the subunit assembly of many proteins in vertebrates and invertebrates. Oligomerization offers functional advantages including multivalency, increased binding strength and the combined function of different domains. These features are seen in natural proteins and may be introduced by protein engineering. The special focus of this review is on oligomerization domain of extracellular matrix proteins. For thrombospondins, initial interesting results on the functional role of oligomerization have been published. Other features remain to be explored. For example, it is not clear why thrombospondin-1 and thrombospondin-2 are trimers whereas thrombospondins-3 to -5 are pentamers. To stimulate this type of research, this review makes a survey of oligomerization domains and their functional role in extracellular matrix proteins.
Engel
Jürgen
J
Department for Biophysical Chemistry, Biozentrum, University of Basel, Basel CH 4056, Switzerland. juergen.engel@unibas.ch
D000595:Amino Acid Sequence; D016326:Extracellular Matrix Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D015202:Protein Engineering; D017434:Protein Structure, Tertiary / Q000235:genetics; D016415:Sequence Alignment; D019699:Thrombospondins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D016326:Extracellular Matrix Proteins; D019699:Thrombospondins