Fibrinogen binding protein: Difference between revisions
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==Structural motifs== | ==Structural motifs== | ||
The overall dimensions of Efb-C were approximately 40x25x20 A° and 15.6 kDa, with the N-terminal a1 helix (K106–H125) connected | The overall dimensions of Efb-C were approximately 40x25x20 A° and 15.6 kDa, with the N-terminal a1 helix (K106–H125) connected | ||
through a short loop to the a2 helix (V127–L139), followed by the C-terminal a3 helix (K145–Q161), and terminating in a random coil conformation. All three helices were packed in a canonical three-helix bundle fold, with most of the nonpolar side chains directed inward.<ref>PMID: 17351618</ref> [http://p8888-ucelinks.cdlib.org.proxy.library.ucsb.edu:2048/sfx_local?&url_ver=Z39.88-2004&rfr_id=info%3Asid%2Fucsb.worldcat.org%3Aworldcat&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&req_dat=%3Csessionid%3E&rfe_dat=%3Caccessionnumber%3E123919124%3C%2Faccessionnumber%3E&rft_id=info%3Aoclcnum%2F123919124&rft_id=urn%3AISSN%3A1529-2908&rft.aulast=Hammel&rft.aufirst=M&rft.atitle=A+structural+basis+for+complement+inhibition+by+Staphylococcus+aureus.&rft.jtitle=Nature+immunology&rft.date=2007&rft.volume=8&rft.issue=4&rft.spage=430&rft.epage=7&rft.issn=1529-2908&rft.genre=article&rft.sici=1529-2908%28200704%298%3A4%3C430%3AASBFCI%3E2.0.TX%3B2-7&req_id=info:rfa/oclc/institutions/211&req_dat=%3Cip%3E128.111.121.42%3C%2Fip%3E&req_id=info%3Arfa%2Foclc%2FInstitutions%2F211 Figure 1] | through a short loop to the a2 helix (V127–L139), followed by the C-terminal a3 helix (K145–Q161), and terminating in a random coil conformation. All three helices were packed in a canonical three-helix bundle fold, with most of the nonpolar side chains directed inward.<ref>PMID: 17351618</ref> [http://p8888-ucelinks.cdlib.org.proxy.library.ucsb.edu:2048/sfx_local?&url_ver=Z39.88-2004&rfr_id=info%3Asid%2Fucsb.worldcat.org%3Aworldcat&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&req_dat=%3Csessionid%3E&rfe_dat=%3Caccessionnumber%3E123919124%3C%2Faccessionnumber%3E&rft_id=info%3Aoclcnum%2F123919124&rft_id=urn%3AISSN%3A1529-2908&rft.aulast=Hammel&rft.aufirst=M&rft.atitle=A+structural+basis+for+complement+inhibition+by+Staphylococcus+aureus.&rft.jtitle=Nature+immunology&rft.date=2007&rft.volume=8&rft.issue=4&rft.spage=430&rft.epage=7&rft.issn=1529-2908&rft.genre=article&rft.sici=1529-2908%28200704%298%3A4%3C430%3AASBFCI%3E2.0.TX%3B2-7&req_id=info:rfa/oclc/institutions/211&req_dat=%3Cip%3E128.111.121.42%3C%2Fip%3E&req_id=info%3Arfa%2Foclc%2FInstitutions%2F211 Figure 1] Many RCA proteins like factor H contain a short consensus repeat or complement-control protein beta-type fold but Efb does not. Its structure is entirely helical and therefore defined a previously unrecognized fold class for complement regulatory proteins. <ref>PMID: 17351618</ref> | ||
==Interactions== | ==Interactions== | ||
