Structural highlights
Function[DAF_HUMAN] This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.[1] Publication Abstract from PubMedEchovirus 7 (EV7) belongs to the enterovirus genus within the family Picornaviridae. Many picornaviruses use IgG-like receptors that bind into the viral canyon and are required to initiate viral uncoating during infection. However, in addition, some of the enteroviruses use an alternative or additional receptor that binds outside the canyon. Decay-accelerating factor (DAF) has been identified as a cellular receptor for EV7. The crystal structure of EV7 has been determined to 3.1 A resolution and used to interpret the 7.2 A resolution cryo-electron microscopy reconstruction of EV7 complexed with DAF. Each DAF binding site on EV7 is near a two-fold icosahedral symmetry axis, which differs from the binding site of DAF on the surface of coxsackievirus B3, indicating independent evolutionary processes by which DAF has been selected as a picornavirus accessory receptor. This suggests that there is an advantage for these viruses to recognize DAF during the initial process of infection. The Interaction of Decay-accelerating Factor with Echovirus 7.,Plevka P, Hafenstein S, Harris KG, Cifuente JO, Zhang Y, Bowman VD, Chipman PR, Bator CM, Lin F, Medof ME, Rossmann MG J Virol. 2010 Sep 29. PMID:20881044[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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