Crystal structures of the human Dysferlin inner DysF domain.
Crystal structures of the human Dysferlin inner DysF domain.
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DOI：
10.1186/1472-6807-14-3
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发表时间：
2014-01-17
影响因子：
--
通讯作者：
Keep NH
中科院分区：
文献类型：
--
作者：
Sula A;Cole AR;Yeats C;Orengo C;Keep NH
Mutations in dysferlin, the first protein linked with the cell membrane repair mechanism, causes a group of muscular dystrophies called dysferlinopathies. Dysferlin is a type two-anchored membrane protein, with a single C terminal trans-membrane helix, and most of the protein lying in cytoplasm. Dysferlin contains several C2 domains and two DysF domains which are nested one inside the other. Many pathogenic point mutations fall in the DysF domain region. We describe the crystal structure of the human dysferlin inner DysF domain with a resolution of 1.9 Ångstroms. Most of the pathogenic mutations are part of aromatic/arginine stacks that hold the domain in a folded conformation. The high resolution of the structure show that these interactions are a mixture of parallel ring/guanadinium stacking, perpendicular H bond stacking and aliphatic chain packing. The high resolution structure of the Dysferlin DysF domain gives a template on which to interpret in detail the pathogenic mutations that lead to disease.
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DOI：
10.1107/s090744491003982x
发表时间：
2011-04
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Evans PR
通讯作者：
Evans PR
影响因子：
3.9
作者：
Guglieri, Michela;Magri, Francesca;Comi, Giacomo R.
通讯作者：
Comi, Giacomo R.
DOI：
10.1107/s0907444909052925
发表时间：
2010-02
期刊：
Acta crystallographica. Section D, Biological crystallography
影响因子：
--
作者：
Adams PD;Afonine PV;Bunkóczi G;Chen VB;Davis IW;Echols N;Headd JJ;Hung LW;Kapral GJ;Grosse-Kunstleve RW;McCoy AJ;Moriarty NW;Oeffner R;Read RJ;Richardson DC;Richardson JS;Terwilliger TC;Zwart PH
通讯作者：
Zwart PH
影响因子：
2.8
作者：
Cagliani, R;Fortunato, F;Comi, GP
通讯作者：
Comi, GP
影响因子：
4.5
作者：
Cho, Hyun-Jung;Sung, Duck Hyun;Kim, Jong-Won
通讯作者：
Kim, Jong-Won