Common topology within a non-collagenous domain of several different collagen types.
The secondary structure of a conserved non-collagenous module in alpha 1(V), alpha 1(XI), alpha 1(IX), alpha 1(XII), alpha 1(XIV) and alpha 1(XVI) collagen chains and in proline- and arginine-rich protein was analyzed using different algorithms. The results predict that a common anti-parallel beta-sheet structure composed of nine consensus beta-strands is present in these non-collagenous modules. A model for the packing of these beta-sheets is proposed which suggests that the predicted beta-sheet structure may be involved in molecular recognition functions.
Moradi-Améli
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M
Institut de Biologie et de Chimie des Protéines, UPR412-CNRS, Lyon, France.
Deléage
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G
Geourjon
C
C
van der Rest
M
M
D000465:Algorithms; D000595:Amino Acid Sequence; D000818:Animals; D003094:Collagen / Q000737:chemistry* / Q000235:genetics; D016384:Consensus Sequence; D018360:Crystallography, X-Ray; D006801:Humans; D008958:Models, Molecular; D008969:Molecular Sequence Data; D015394:Molecular Structure; D017510:Protein Folding; D017433:Protein Structure, Secondary; D017386:Sequence Homology, Amino Acid
D003094:Collagen