## Abstract Previously we demonstrated by random saturation mutagenesis a set of mutations in the extracellular (EC) loops that constitutively activate the C5a receptor (C5aR) (Klco et al., Nat Struct Mol Biol 2005;12:320β326; Klco et al., J Biol Chem 2006;281:12010β12019). In this study, molecular
Conformational Movement of F251 Contributes to the Molecular Mechanism of Constitutive Activation in the C5a Receptor
β Scribed by Saurabh Sen; Thomas J. Baranski; Gregory V. Nikiforovich
- Book ID
- 111368519
- Publisher
- John Wiley and Sons
- Year
- 2008
- Tongue
- English
- Weight
- 216 KB
- Volume
- 71
- Category
- Article
- ISSN
- 1747-0277
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## Abstract Molecular modeling of conformational changes occurring in the transmembrane region of the complement factor 5a receptor (C5aR) during receptor activation was performed by comparing two constitutively active mutants (CAMs) of C5aR, NQ (I124N/L127Q), and F251A, to those of the wildβtype C
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