Fibrinogen binding protein: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 17: | Line 17: | ||
Two amino acids of Efb were noted as extremely important in achieving binding with the C3d domain, R131 and N138. Mutations by site -directed mutagenesis to these two points showed lack of complex formation and showed that other residues of Efb were not enough to drive complex formation. It was also observed that the a2 helix was mostly interacting with the C3d complex.<br> | Two amino acids of Efb were noted as extremely important in achieving binding with the C3d domain, R131 and N138. Mutations by site -directed mutagenesis to these two points showed lack of complex formation and showed that other residues of Efb were not enough to drive complex formation. It was also observed that the a2 helix was mostly interacting with the C3d complex.<br> | ||
Efb-C blocks the formation of the functional C3b opsonin by binding tightly to the thioester-containing domain of native C3 and by perturbing the overall solution conformation of the molecule to one that is incapable of being processed into C3b. <ref>PMID: 17351618</ref> | Efb-C blocks the formation of the functional C3b opsonin by binding tightly to the thioester-containing domain of native C3 and by perturbing the overall solution conformation of the molecule to one that is incapable of being processed into C3b. <ref>PMID: 17351618</ref> | ||
==Future Possibilities== | ==Future Possibilities== | ||
Possible new anti-staph. aureus compounds can be synthesized that target the Efb-C3 interaction. It can also be used as a model in clinical settings to block complement activation. Knowing the two binding sites, R131 and N138, is a good starting point for screening of new bioactive peptides. <ref>PMID: 17351618</ref> | Possible new anti-staph. aureus compounds can be synthesized that target the Efb-C3 interaction. It can also be used as a model in clinical settings to block complement activation. Knowing the two binding sites, R131 and N138, is a good starting point for screening of new bioactive peptides. <ref>PMID: 17351618</ref> | ||
</StructureSection> | </StructureSection> | ||
