Prokaryotic collagen-like proteins and uses thereof

Chemistry: natural resins or derivatives; peptides or proteins; – Proteins – i.e. – more than 100 amino acid residues – Scleroproteins – e.g. – fibroin – elastin – silk – etc.

Reexamination Certificate

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C530S350000

Reexamination Certificate

active

06953839

ABSTRACT:
The present invention provides recombinant triple helical proteins or collagen-like proteins comprising a prokaryotic protein or one or more domains of a prokaryotic protein comprising a collagen-like peptide sequence of repeated Gly-Xaa-Yaa triplets and, optionally, one or more domains from a mammalian collagen. Also provided are expression vectors and host cells containing the expression vectors to produce these recombinant proteins and methods of production for the same. Additionally, antibodies are provided that are directed against a recombinant collagen-like protein that, preferably, binds an integrin. Furthermore, a method of screening for potential therapeutic compounds that inhibit the integrin-binding or -interacting activities of recombinant collagen-like proteins.

REFERENCES:
Xu et al., “Streptococcal Scl1 and Scl2 proteins from collagen-like triple helices”, 2002, The Journal of Biological Chemistry, 277(30), 27312-18.
Apte et al., “Cloning of the human and mouse type X collagen genes and mapping of the mouse type X collagen gen to chromosome 10”, 1992, Eupopean Journal of Biochemistry, 206, 217-224.
Wells, “Additivity of Mutational Effects in Proteins”, 1990, Biochemistry, 29(37), 8509-8517.
GenBank sequence for AF296333, Nov. 06, 2000.
Bowie et al., “Deciphering the message in protein sequences: Tolerance to amino acid substitutions”, 1990, Science, 247, 1306-1310.

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