| First Author | Matsubara M | Year | 1998 |
| Journal | FEBS Lett | Volume | 421 |
| Issue | 3 | Pages | 203-7 |
| PubMed ID | 9468306 | Mgi Jnum | J:352563 |
| Mgi Id | MGI:7707618 | Doi | 10.1016/s0014-5793(97)01557-3 |
| Citation | Matsubara M, et al. (1998) MARCKS, a major protein kinase C substrate, assumes non-helical conformations both in solution and in complex with Ca2+-calmodulin. FEBS Lett 421(3):203-7 |
| abstractText | MARCKS, a major cellular substrate for protein kinase C, plays important roles in various cellular functions and its functions are regulated by calmodulin. We have studied the conformational properties of recombinant human MARCKS in solution and in complex with calmodulin. Circular dichroism (CD) spectra showed a high content of random coil in physiological solution. When MARCKS or MARCKS-derived calmodulin-binding peptide was complexed with Ca2+-calmodulin, little change was observed in the CD spectra, suggesting that MARCKS binds with calmodulin in a non-helical conformation, which is unique among the calmodulin-binding proteins. |
