期刊
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
卷 1784, 期 9, 页码 1265-1270出版社
ELSEVIER
DOI: 10.1016/j.bbapap.2008.05.005
关键词
calreticulin; SAXS; protein folding; chaperone; endoplasmic reticulum
资金
- Biological Macromolecules, EMBL Outstation Hamburg
- Dept. of Medicinal Chemistry
- University of Copenhagen
- Carlsberg Research Foundation
- Novo Nordisk A/S
- Novo Nordisk Foundation
- Dept of Nano-and Microelectronics
- The Danish Technical University
- The Danish Medical Research Council
- DANSYNC
Calreticulin plays a central role in vital cell processes such as protein folding, Ca2+ homeostasis and immunogenicity. Even so, only limited three-dimensional structural information is presently available. We present a series of Small-Angle X-ray Scattering data on human placenta calreticulin. The data from the calreticulin monomer reveal the shape of calreticulin in solution: The previously structurally un-described C-terminal is seen as a globular domain, and the P-domain P-hairpin extends from the N-domain in a spiral like conformation. In the calreticulin solution dimer, the N-, C-, and P-domains are easily identified, and the P-domain is in an extended conformation connecting to the second calreticulin molecule. The SAXS solution data enables the construction of a medium-resolution model of calreticulin. In the light of the unresolved chaperone mechanism of calreticulin and calnexin,we discuss the functional consequences of the conformational plasticity of the calreticulin P-domain. (c) 2008 Elsevier B.V. All rights reserved.
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