Complement Regulator-Acquiring Surface Protein: Difference between revisions

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=== '''Relation to the Extra Cellular Matrix''' ===
=== '''Relation to the Extra Cellular Matrix''' ===


Recently it was found that BbCRASP-1 not only binds to FH and FHL-1 proteins, but it also binds to several other human ligands such as [http://www.uniprot.org/uniprot/BMP2_HUMAN BMP-2] and Extra cellular matrix ligands Collagen I, Collagen III, Collagen IV, fibronectin, laminin, and plasminogen (Hallstrom et al. 2010). As a result of this new  finding, BbCRASP-1 is said to advocate the bypassing of the complementary immune system in addition to the pathogenesis of Lyme disease. BbCRASP-1 facilitates binding of “Borrelia burgdoferi” to human cells and tissues, which helps spread the infection (Hallstrom et al. 2010).
Recently it was found that BbCRASP-1 not only binds to FH and FHL-1 proteins, but it also binds to several other human ligands such as [http://www.uniprot.org/uniprot/BMP2_HUMAN BMP-2] and Extra cellular matrix ligands Collagen I, Collagen III, Collagen IV, fibronectin, laminin, and plasminogen <ref name"Hallstrom">PMID: 20565259</ref>. As a result of this new  finding, BbCRASP-1 is said to advocate the bypassing of the complementary immune system in addition to the pathogenesis of Lyme disease. BbCRASP-1 facilitates binding of “Borrelia burgdoferi” to human cells and tissues, which helps spread the infection (Hallstrom et al. 2010).




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=== '''Other Potential Binding Sites''' ===
=== '''Other Potential Binding Sites''' ===


Additional studies were done to investigate the FH and FHL-1 binding sites on the protein. As with previous research, areas of high conservation were investigated due to their relationship with upholding the structure and function of the protein <ref name="Cordes 06">PMID: 16530476</ref>. Researchers examined highly conserved areas of amino acid sequences along the <scene name='SB2013_L01gr6/Pocket_region/1'>cleft region</scene> of the protein. They saw that the majority of these regions clustered on a highly-exposed region of the protein.
Additional studies were done to investigate the FH and FHL-1 binding sites on the protein. As with previous research, areas of high conservation were investigated due to their relationship with upholding the structure and function of the protein <ref name="CordesF">PMID: 16530476</ref>. Researchers examined highly conserved areas of amino acid sequences along the <scene name='SB2013_L01gr6/Pocket_region/1'>cleft region</scene> of the protein. They saw that the majority of these regions clustered on a highly-exposed region of the protein.




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