The Pla Alloantigen System Is a Sensitive Indicator of the Structural Integrity of the Amino-terminal Domain of the Human Integrin β3 Subunit
TJ Kunicki, S Honda, B Dawson, Y Honda… - Blood Cells, Molecules …, 1995 - Elsevier
Within the native integrin αIIbβ3, the conformation of the amino-terminal domain of the β3
subunit has a significant influence on the availability of the Leu33/Pro33 polymorphism that
defines the A1 and A2 alleles, respectively, of the PlA alloantigen system. The majority of
anti-PlA1 IgG antibodies, affinity-purified by adsorption to either (A1/A1)-platelets or purified
αIIb (A1) β3, fail to bind to the Leu33 polymorphic loop within Cys26-Cys38 in native β3
unless this sequence is maintained in a proper orientation by two noncontiguous human β3 …
subunit has a significant influence on the availability of the Leu33/Pro33 polymorphism that
defines the A1 and A2 alleles, respectively, of the PlA alloantigen system. The majority of
anti-PlA1 IgG antibodies, affinity-purified by adsorption to either (A1/A1)-platelets or purified
αIIb (A1) β3, fail to bind to the Leu33 polymorphic loop within Cys26-Cys38 in native β3
unless this sequence is maintained in a proper orientation by two noncontiguous human β3 …