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| | <StructureSection load='4cah' size='340' side='right'caption='[[4cah]], [[Resolution|resolution]] 1.90Å' scene=''> | | <StructureSection load='4cah' size='340' side='right'caption='[[4cah]], [[Resolution|resolution]] 1.90Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4cah]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CAH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4CAH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4cah]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4CAH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CAH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.901Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4cai|4cai]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4cah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cah OCA], [http://pdbe.org/4cah PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4cah RCSB], [http://www.ebi.ac.uk/pdbsum/4cah PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4cah ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4cah FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cah OCA], [https://pdbe.org/4cah PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cah RCSB], [https://www.ebi.ac.uk/pdbsum/4cah PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cah ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/DYSF_HUMAN DYSF_HUMAN]] Miyoshi myopathy;Distal myopathy with anterior tibial onset;Congenital myopathy, Paradas type;Autosomal recessive limb-girdle muscular dystrophy type 2B. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. | + | [https://www.uniprot.org/uniprot/DYSF_HUMAN DYSF_HUMAN] Miyoshi myopathy;Distal myopathy with anterior tibial onset;Congenital myopathy, Paradas type;Autosomal recessive limb-girdle muscular dystrophy type 2B. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/DYSF_HUMAN DYSF_HUMAN]] Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity). | + | [https://www.uniprot.org/uniprot/DYSF_HUMAN DYSF_HUMAN] Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Cole, A R]] | + | [[Category: Cole AR]] |
| - | [[Category: Keep, N H]] | + | [[Category: Keep NH]] |
| - | [[Category: Orengo, C]] | + | [[Category: Orengo C]] |
| - | [[Category: Sula, A]] | + | [[Category: Sula A]] |
| - | [[Category: Yeats, C]] | + | [[Category: Yeats C]] |
| - | [[Category: Dysf domain]]
| + | |
| - | [[Category: Limb-girdle muscular dystrophy]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Membrane repair]]
| + | |
| Structural highlights
Disease
DYSF_HUMAN Miyoshi myopathy;Distal myopathy with anterior tibial onset;Congenital myopathy, Paradas type;Autosomal recessive limb-girdle muscular dystrophy type 2B. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry. The disease is caused by mutations affecting the gene represented in this entry.
Function
DYSF_HUMAN Key calcium ion sensor involved in the Ca(2+)-triggered synaptic vesicle-plasma membrane fusion. Plays a role in the sarcolemma repair mechanism of both skeletal muscle and cardiomyocytes that permits rapid resealing of membranes disrupted by mechanical stress (By similarity).
Publication Abstract from PubMed
BACKGROUND: 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. RESULTS: We describe the crystal structure of the human dysferlin inner DysF domain with a resolution of 1.9 Angstroms. 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. CONCLUSIONS: 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.
Crystal structures of the human Dysferlin inner DysF domain.,Sula A, Cole AR, Yeats C, Orengo C, Keep NH BMC Struct Biol. 2014 Jan 17;14(1):3. doi: 10.1186/1472-6807-14-3. PMID:24438169[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Sula A, Cole AR, Yeats C, Orengo C, Keep NH. Crystal structures of the human Dysferlin inner DysF domain. BMC Struct Biol. 2014 Jan 17;14(1):3. doi: 10.1186/1472-6807-14-3. PMID:24438169 doi:http://dx.doi.org/10.1186/1472-6807-14-3
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