Adey N B, Kay B K
Department of Biology, University of North Carolina, Chapel Hill, 27599-3280, USA.
Gene. 1996 Feb 22;169(1):133-4. doi: 10.1016/0378-1119(95)00804-7.
The calcium-binding protein, calmodulin (CaM), was used to screen a phage library displaying random peptides 26 amino acids (aa) in length. Twenty CaM-binding peptides were identified, 17 of which contained one of three consensus sequence motifs: + W-OlambdaR, WRAAV or WRXXAAAL, where +, -, O, lambda and X are positively charged, negatively charged, hydrophobic, leucine or valine, and any residue, respectively. The Trp residue in these motifs is located within 14 aa of the N-terminus of the displayed peptide. Previous studies [Dedman et al., J. Biol. Chem. 268 (1993) 23025-23030] using a library displaying random peptides 15 aa in length identified CaM-binding peptides which contained a Trp-Pro dipeptide motif. These results suggest that the type of CaM-binding motif identified can vary between different types of combinatorial peptides.
钙结合蛋白钙调蛋白（CaM）被用于筛选展示长度为26个氨基酸（aa）的随机肽的噬菌体文库。鉴定出了20个CaM结合肽，其中17个包含三个共有序列基序之一：+W-OλR、WRAAV或WRXXAAAL，其中+、-、O、λ和X分别是带正电荷、带负电荷、疏水、亮氨酸或缬氨酸以及任意残基。这些基序中的色氨酸残基位于所展示肽N端的14个氨基酸范围内。先前的研究[戴德曼等人，《生物化学杂志》268（1993）23025 - 23030]使用展示长度为15个氨基酸的随机肽的文库鉴定出了包含色氨酸-脯氨酸二肽基序的CaM结合肽。这些结果表明，所鉴定的CaM结合基序类型在不同类型的组合肽之间可能会有所不同。
