| Autor: |
Podol'nikova NP; Palladin Institute of Biochemistry, National Academy of Sciences of Ukraine, Kyiv., Volkov HL, Uharova TP |
| Jazyk: |
ukrajinština |
| Zdroj: |
Ukrains'kyi biokhimichnyi zhurnal (1999 ) [Ukr Biokhim Zh (1999)] 2003 Nov-Dec; Vol. 75 (6), pp. 99-105. |
| Abstrakt: |
The interactions between platelet integrin alpha IIb beta 3 and fibrinogen (Fg) mediate a range of adhesive reactions, which are necessary for platelet aggregation and fibrin clot retraction. The binding site for alpha IIb beta 3 resides in the gamma C domain of Fg. In our previous work we have identified a novel binding site in the gamma C domain, gamma 370-383 (P3), for integrin alpha IIb beta 3 and have demonstrated that the P3 sequence together with the C-terminal gamma C sequence 408AGDV411 accounts for the full binding of alpha IIb beta 3. In our present study, in order to define the amino acid residues in P3 involved in the interaction with alpha IIb beta 3, we have used SPOT-synthesis analyses. Libraries consisting of peptides covering P3 were created and probed with radiolabeled alpha IIb beta 3. Screening of the libraries showed that several positively charged residues may be critical for interaction of P3 with integrin alpha IIb beta 3. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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