G1SecL05: Difference between revisions
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LA-2 fab recognizes the three surface-exposed loops; loop1, loop 2 and loop 3 of the C-terminal domain of OspA that are on the tip of the elongated molecule most distant from the lipid-modified N terminus. Residues 203 to 220 in “loop 1“ , residues 224 to 233 in “loop 2“ and residues 246 to 257 in “loop 3“are mostly effected by la-2 binding. In loop 1 residues 206 and 216 are not affected. The interactions between OspA and LA-2 include eight direct hydrogen bonds, four solvent-bridged hydrogen bonds, three ion pairs, and numerous van der Waals interactions.<ref>•Ding W, Huang X, Yang X, Dunn JJ, Luft BJ, Koide S, Lawson CL. Structural identification of a key protective B-cell epitope in Lyme disease antigen OspA. J Mol Biol. 2000 Oct 6;302(5):1153-64.PMID:11183781 doi:10.1006/jmbi.2000.4119 | LA-2 fab recognizes the three surface-exposed loops; loop1, loop 2 and loop 3 of the C-terminal domain of OspA that are on the tip of the elongated molecule most distant from the lipid-modified N terminus. Residues 203 to 220 in “loop 1“ , residues 224 to 233 in “loop 2“ and residues 246 to 257 in “loop 3“are mostly effected by la-2 binding. In loop 1 residues 206 and 216 are not affected. The interactions between OspA and LA-2 include eight direct hydrogen bonds, four solvent-bridged hydrogen bonds, three ion pairs, and numerous van der Waals interactions.<ref>•Ding W, Huang X, Yang X, Dunn JJ, Luft BJ, Koide S, Lawson CL. Structural identification of a key protective B-cell epitope in Lyme disease antigen OspA. J Mol Biol. 2000 Oct 6;302(5):1153-64.PMID:11183781 doi:10.1006/jmbi.2000.4119 | ||
</ref> | </ref> | ||
<Structure load='1FJ1' size='400' frame='true' align='right' scene='Studio:G1SecL01/2/1' /> | |||
==Limitations == | ==Limitations == | ||
