Spectrin, subunit alpha

displayed: apo-spectrin in green, Ca2+-spectrin in cyan (structures from A Pastore).
 
The alpha subunit of spectrin contains two EF-hands that bind Ca2+ with non-physiological affinity in vitro.  Both undergo moderate conformational change, although it has been proposed that Ca2+ binding is sequential; EF2 (green and cyan cylinders on right) must bind Ca2+ before EF1 can bind.  Interestingly, the movement of EF2 has been attributed to side-to-side packing with EF1, since EF2 itself lacks the hydrophobic core and aromatic residues key to the conformational change observed in EF1.

 
EF-hand (helix residues) N-terminal coordinate
of second helix
theta phi omega
apo-spectrin EF1 (14-21, 31-41) (10.228, 0.179, -2.019) 47.343 117.007 102
apo-spectrin EF2 (57-64, 74-84) (5.662, 7.792, -4.203) 34.003 134.368 51
Ca2+-spectrin EF1 (14-21, 31-41) (6.803, -0.715, -5.806) 47.217 69.474 92
Ca2+-spectrin EF2 (57-64, 74-84) (6.246, 2.524, -7.194) 70.576 129.539 65

 

NB: values obtained using apo-CaM EF1 (as in refcam.pdb) as the reference EF-hand.


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