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Table 3 Comparison of interface residues of avidin, putative BBPs and AVR-proteins. Residues at subunit interfaces in avidin are determined according to Livnah et al. [17]. Equivalent residues in the other proteins are shown based on their alignment.

From: Chicken genome analysis reveals novel genes encoding biotin-binding proteins related to avidin family

Secondary structure and type of interaction of amino acid residues of avidin in different subunit interfaces Residue in avidin Differences found in other proteins
Secondary M-chain S-chain   BBP-A BBP-B AVRsa
1–4 interface
β4 H-bonds   H50 Kb Rc L
β4 H-bond   Q53 - - -
β4   H-bonds N54 Qd Qd H
B4 H-bond H-bond T55 Pb Qb gap
L4   H-bond N57 Td Sd K
L4   H-bonds R59 Gb Vb A
β5 H-bond   G65 - Ad -
β5 H-bond H-bond T67 - - -
β5   H-bonds N69 Qe Wf L/H
L5 H-bonds   W70 - - -
L5   H-bond K71 Qd Db N
L5 H-bonds   S73 Ad - -
β6   H-phobic V78 - Ad -
β6 H-bond   T80 Vf Af V
β6   H-bonds Q82 - - -
β7 H-bond   M96 Ab Tb K
β7   H-phobic L98 - Md -
β7   H-bond R100 - - -
β7 H-bond   S101 Eg Eg L
L7 H-bond   V103 - - -
β8   H-bonds T113 - - -
1–2 interface
L7   H-phobic W110 - - -
B8 H-bond   T113 - - -
B8 H-bond   V115 - - -
1–3 interface
B7 H-bond H-phobic M96 A Tb K
B8   H-phobic V115 - - -
B8   H-phobic I117 T Rh N/Y
  1. aDifferences found in all AVR-proteins 1–7 in previous studies [27, 31] and current study (AVR-A, B, C)
  2. bNo interaction according to the model
  3. cSalt bridge to D26 in subunit 4 according to the model
  4. dInteraction similar to avidin according to the model
  5. eInteraction similar to avidin without linking water molecule according to the model
  6. fHydrophobic interaction according to the model
  7. gSide-chain hydrogen bond according to the model
  8. hSalt bridge to E13 in subunit 3 according to the model