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. Author manuscript; available in PMC: 2012 Apr 19.
Published in final edited form as: J Biol Chem. 2008 Sep 26;283(47):32704–32714. doi: 10.1074/jbc.M802066200

Table II.

Cation-binding sites in the β1 and β3 A domains and their coordinating residues. Cation-binding site mutants made in β1 are shown in bold. Mutations were based on β3 structure as identified in the aVβ3 crystal structures. The cation-coordinating residues in β3 are shown alongside the corresponding residues in β1. Coordinating residues found only in the unliganded structure are marked with ‘*’ (12) and those found only in the liganded structure are marked with ‘**’ (13).

Cation
binding site
Residues
MIDAS β3 Asp119 Ser121 Ser123 Glu220 Asp251
β1 Asp130 Ser132 Ser134 Glu229 Asp259
mutation D130A
ADMIDAS β3 Ser123 Asp126 Asp127 Met335* Asp251**
β1 Ser134 Asp137 Asp138 Ala341 Asp259
mutation D137A D138A
LIMBS β3 Asp158 Asn215 Asp217 Pro219 Glu220
β1 Glu169 Asn224 Asp226 Pro228 Glu229
mutation E169A
E169D
D226A