| First Author | Yamauchi E | Year | 2003 |
| Journal | Nat Struct Biol | Volume | 10 |
| Issue | 3 | Pages | 226-31 |
| PubMed ID | 12577052 | Mgi Jnum | J:168209 |
| Mgi Id | MGI:4887342 | Doi | 10.1038/nsb900 |
| Citation | Yamauchi E, et al. (2003) Crystal structure of a MARCKS peptide containing the calmodulin-binding domain in complex with Ca2+-calmodulin. Nat Struct Biol 10(3):226-31 |
| abstractText | The calmodulin-binding domain of myristoylated alanine-rich C kinase substrate (MARCKS), which interacts with various targets including calmodulin, actin and membrane lipids, has been suggested to function as a crosstalk point among several signal transduction pathways. We present here the crystal structure at 2 A resolution of a peptide consisting of the MARCKS calmodulin (CaM)-binding domain in complex with Ca2+-CaM. The domain assumes a flexible conformation, and the hydrophobic pocket of the calmodulin N-lobe, which is a common CaM-binding site observed in previously resolved Ca2+-CaM-target peptide complexes, is not involved in the interaction. The present structure presents a novel target-recognition mode of calmodulin and provides insight into the structural basis of the flexible interaction module of MARCKS. |
