Binding of APC‐derived C‐terminal peptides to EB1‐C.

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Binding of APC‐derived C‐terminal peptides to EB1‐C. Binding of APC‐derived C‐terminal peptides to EB1‐C. (A) Sequence alignment of carboxy‐terminal APC segments from different species. Sequence identities and accession numbers are as follows: hs, Homo sapiens, SwissProt: P25054; rn, Rattus norvegicus, SwissProt: P70478; xl, Xenopus laevis, TrEMBL: P70039; sc, Saccharomyces cerevisiae, SwissProt: P32526. Conserved residues are depicted in bold. The thick line indicates the C‐APCp1 peptide sequence (Val2781–Lys2819). The hsAPC Ile2805–Pro2806 dipeptide segment that was targeted for substitution and the Cdc2 consensus site Ser2789–Lys2792 are underlined. (B) ITC binding study. Left panel: Integrated heats of reaction (symbols) with the best fit to the data (lines). The fits were obtained with n=1 (referred to the EB1‐C monomer) and yielded equilibrium dissociation constants of KD=5.1 (ΔH0app=−21.1 kcal/mol binding sites) and 17.9 μM (ΔH0app=−19.5 kcal/mol binding sites) for C‐APCp1 (closed symbols) and C‐pAPCp1 (phosphorylated at Ser2789; open symbols), respectively. Inset: Raw data obtained for 30 10 μl injections of C‐APCp1 (1000 μM) into the sample cell containing 90 μM EB1‐C. Right upper panel: Raw data obtained for C‐APCp1‐S (800 μM) into EB1‐C (90 μM). Right lower panel: Raw data obtained for C‐APCp2 (970 μM) into EB1‐C (90 μM). The measurements were carried out at 25°C in PBS. The concentrations of EB1‐C refer to the monomer. Srinivas Honnappa et al. EMBO J. 2005;24:261-269 © as stated in the article, figure or figure legend