Skip to main content

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