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2yle
From Proteopedia
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==Crystal structure of the human Spir-1 KIND FSI domain in complex with the FSI peptide== | ==Crystal structure of the human Spir-1 KIND FSI domain in complex with the FSI peptide== | ||
| - | <StructureSection load='2yle' size='340' side='right' caption='[[2yle]], [[Resolution|resolution]] 1.80Å' scene=''> | + | <StructureSection load='2yle' size='340' side='right'caption='[[2yle]], [[Resolution|resolution]] 1.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2yle]] is a 2 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2yle]] is a 2 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=2YLE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2YLE FirstGlance]. <br> |
| - | </td></tr><tr><td class="sblockLbl"><b>[[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2yle FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2yle OCA], [https://pdbe.org/2yle PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2yle RCSB], [https://www.ebi.ac.uk/pdbsum/2yle PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2yle ProSAT]</span></td></tr> |
| - | <table> | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SPIR1_HUMAN SPIR1_HUMAN] Acts as a actin nucleation factor, remains associated with the slow-growing pointed end of the new filament. Involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. Required for asymmetric spindle positioning and asymmetric cell division during meiosis. Required for normal formation of the cleavage furrow and for polar body extrusion during female germ cell meiosis.<ref>PMID:11747823</ref> <ref>PMID:21620703</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
| + | <div class="pdbe-citations 2yle" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Kerkhoff | + | [[Category: Large Structures]] |
| - | [[Category: Pechlivanis | + | [[Category: Kerkhoff E]] |
| - | [[Category: Vonrhein | + | [[Category: Pechlivanis M]] |
| - | [[Category: Zeth | + | [[Category: Vonrhein C]] |
| - | + | [[Category: Zeth K]] | |
| - | + | ||
Current revision
Crystal structure of the human Spir-1 KIND FSI domain in complex with the FSI peptide
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