Mutations in and near the second calcium-binding domain of integrin alphaIIb affect the structure and function of integrin alphaIIbbeta3.

ABSTRACT: Calcium-binding domains in the alpha-subunit of integrins contain a central loop structure. To examine the importance of the loop structure, a series of alphaIIb mutants containing changes to the calcium-liganding amino acids have been constructed. Significantly, none of the mutant alphaIIbbeta3 complexes was detected on the surface of transfected cells, but mutant pro-alphaIIb was detected in cell lysates in complex with beta3. To study the importance of the regions flanking the second calcium-binding domain for ligand-binding and ligand-binding specificity, three alphaIIb/alpha5 chimaeras containing alpha5 sequences flanking or flanking and including the second calcium-binding domain were constructed. The chimaera containing both alpha5-flanking regions was not expressed on the cell surf

SUBMITTER: Gidwitz S 

PROVIDER: S-EPMC1224065 | biostudies-literature | 2004 Apr

REPOSITORIES: biostudies-literature