Structural characterization of the second TSP1-module of human thrombospondin

The TSP1-module has been first identified as the type 1 repeat of thrombospondin-1. Members of this extracellular module-family have since been shown to be present in several hundred metazoan proteins as well as in proteins of some protists. Despite the widespread occurrence and biological importanc...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2002-08, Vol.296 (1), p.156-160
Main Authors: Roszmusz, Emőke, Patthy, András, Trexler, Mária, Patthy, László
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Circular Dichroism
Circular dichroism spectroscopy
Cloning, Molecular
Disulfide connectivity
DNA Primers
Escherichia coli
Humans
Metazoa
Midkine
Molecular Sequence Data
Pleiotrophin
Properdin
Recombinant Proteins - chemistry
Recombinant Proteins - genetics
Sequence Homology, Amino Acid
Spectrophotometry, Ultraviolet
Thrombospondin
Thrombospondins - chemistry
Thrombospondins - genetics
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Summary:The TSP1-module has been first identified as the type 1 repeat of thrombospondin-1. Members of this extracellular module-family have since been shown to be present in several hundred metazoan proteins as well as in proteins of some protists. Despite the widespread occurrence and biological importance of this module-type, relatively little is known about their three-dimensional structure. To define the structural features of this important module-family, we have expressed the second TSP1-domain of human thrombospondin 1 in Escherichia coli. Amino acid sequencing of proteolytic fragments of the recombinant protein have shown that its disulfide bonds connect the six conserved cysteines in a 1–5, 2–6, 3–4 pattern. Circular dichroism studies on the recombinant protein indicate that the disulfide-bonded TSP1-module consists primarily of distorted β-strands.
ISSN:0006-291X
1090-2104
DOI:10.1016/S0006-291X(02)00826-4