کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5372053 | 1503976 | 2007 | 7 صفحه PDF | دانلود رایگان |

p65/L-Plastin is a leukocyte-specific EF-hand protein which plays a vital role in organizing the actin cytoskeleton. Since its overall structural information has been largely unknown, we employed the X-ray scattering technique to elucidate the structure. Kratky plots of p65/l-plastin showed one peak, indicating that the protein takes compact globular conformations. The radii of gyration (Rg) of the monomer p65/l-plastin estimated from Guinier plots were 27.5 ± 0.5 à and 28.6 à in the absence and presence of Ca2+, respectively. The distance distribution function P(r) gave single peaks at 31.5-32.3 à and 33 à in the absence and presence of Ca2+, respectively. These indicate that p65/l-plastin becomes somewhat larger in the presence of Ca2+. The molecular shape of p65/l-plastin reconstructed from X-ray scattering data using the DAMMIN program has provided the first view of the overall structure of full-length plastin/fimbrin family proteins: a compact horseshoe-like shape with a small projection, which also exhibits Ca2+-induced conformational changes.
Journal: Biophysical Chemistry - Volume 131, Issues 1â3, December 2007, Pages 36-42