Unknown

Dataset Information

0

The skeletal muscle Ca2+ release channel has an oxidoreductase-like domain.


ABSTRACT: We used a combination of bioinformatics, electron cryomicroscopy, and biochemical techniques to identify an oxidoreductase-like domain in the skeletal muscle Ca2+ release channel protein (RyR1). The initial prediction was derived from sequence-based fold recognition for the N-terminal region (41-420) of RyR1. The putative domain was computationally localized to the clamp domain in the cytoplasmic region of a 22A structure of RyR1. This localization was subsequently confirmed by difference imaging with a sequence specific antibody. Consistent with the prediction of an oxidoreductase domain, RyR1 binds [3H]NAD+, supporting a model in which RyR1 has a oxidoreductase-like domain that could function as a type of redox sensor.

SUBMITTER: Baker ML 

PROVIDER: S-EPMC129414 | biostudies-literature | 2002 Sep

REPOSITORIES: biostudies-literature

altmetric image

Publications

The skeletal muscle Ca2+ release channel has an oxidoreductase-like domain.

Baker Matthew L ML   Serysheva Irina I II   Sencer Serap S   Wu Yili Y   Ludtke Steven J SJ   Jiang Wen W   Hamilton Susan L SL   Chiu Wah W  

Proceedings of the National Academy of Sciences of the United States of America 20020906 19


We used a combination of bioinformatics, electron cryomicroscopy, and biochemical techniques to identify an oxidoreductase-like domain in the skeletal muscle Ca2+ release channel protein (RyR1). The initial prediction was derived from sequence-based fold recognition for the N-terminal region (41-420) of RyR1. The putative domain was computationally localized to the clamp domain in the cytoplasmic region of a 22A structure of RyR1. This localization was subsequently confirmed by difference imagin  ...[more]

Similar Datasets

| S-EPMC3961684 | biostudies-literature
| S-EPMC6302159 | biostudies-literature
| S-EPMC4742110 | biostudies-literature
| S-EPMC4873205 | biostudies-literature
| S-EPMC5748219 | biostudies-literature
| S-EPMC4735524 | biostudies-literature