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| | <StructureSection load='7bqi' size='340' side='right'caption='[[7bqi]], [[Resolution|resolution]] 1.30Å' scene=''> | | <StructureSection load='7bqi' size='340' side='right'caption='[[7bqi]], [[Resolution|resolution]] 1.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[7bqi]] 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=7BQI OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=7BQI FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[7bqi]] 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=7BQI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BQI FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FYCO1, ZFYVE7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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]] 1.3Å</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=7bqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bqi OCA], [http://pdbe.org/7bqi PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=7bqi RCSB], [http://www.ebi.ac.uk/pdbsum/7bqi PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=7bqi 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=7bqi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bqi OCA], [https://pdbe.org/7bqi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bqi RCSB], [https://www.ebi.ac.uk/pdbsum/7bqi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bqi ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Disease == | | == Disease == |
| - | [[http://www.uniprot.org/uniprot/FYCO1_HUMAN FYCO1_HUMAN]] Nuclear cataract. The disease is caused by mutations affecting the gene represented in this entry. Pathogenic mutations in FYCO1 can affect intracellular transport of autophagocytic vesicles from the perinuclear area to the periphery, leading to an accumulation of large numbers of vesicles and hence loss of lens transparency (PubMed:21636066).<ref>PMID:21636066</ref> | + | [https://www.uniprot.org/uniprot/FYCO1_HUMAN FYCO1_HUMAN] Nuclear cataract. The disease is caused by mutations affecting the gene represented in this entry. Pathogenic mutations in FYCO1 can affect intracellular transport of autophagocytic vesicles from the perinuclear area to the periphery, leading to an accumulation of large numbers of vesicles and hence loss of lens transparency (PubMed:21636066).<ref>PMID:21636066</ref> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/FYCO1_HUMAN FYCO1_HUMAN]] May mediate microtubule plus end-directed vesicle transport.<ref>PMID:20100911</ref> | + | [https://www.uniprot.org/uniprot/FYCO1_HUMAN FYCO1_HUMAN] May mediate microtubule plus end-directed vesicle transport.<ref>PMID:20100911</ref> |
| - | <div style="background-color:#fffaf0;">
| + | |
| - | == Publication Abstract from PubMed ==
| + | |
| - | FYCO1 is a multidomain adaptor protein that plays an important role in autophagy by mediating the kinesin-dependent microtubule plus-end-directed transport of autophagosomes. FYCO1 contains a RUN domain, which is hypothesized to function as a specific effector for members of the Ras superfamily of small GTPases, but its role has not been well characterized and its interaction partner(s) have not been identified. Here, the crystal structure of the FYCO1 RUN domain was determined at 1.3 A resolution. The overall structure of the FYCO1 RUN domain was similar to those of previously reported RUN domains. Detailed structural comparisons with other RUN domains and docking studies suggested a possible interaction interface of the FYCO1 RUN domain with small GTPases of the Ras superfamily.
| + | |
| - | | + | |
| - | Crystal structure of the FYCO1 RUN domain suggests possible interfaces with small GTPases.,Sakurai S, Shimizu T, Ohto U Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):326-333. doi:, 10.1107/S2053230X20009012. Epub 2020 Jul 28. PMID:32744243<ref>PMID:32744243</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 7bqi" style="background-color:#fffaf0;"></div>
| + | |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ohto, U]] | + | [[Category: Ohto U]] |
| - | [[Category: Sakurai, S]] | + | [[Category: Sakurai S]] |
| - | [[Category: Shimizu, T]] | + | [[Category: Shimizu T]] |
| - | [[Category: Autophagy]]
| + | |
| - | [[Category: Cytosolic protein]]
| + | |
| Structural highlights
Disease
FYCO1_HUMAN Nuclear cataract. The disease is caused by mutations affecting the gene represented in this entry. Pathogenic mutations in FYCO1 can affect intracellular transport of autophagocytic vesicles from the perinuclear area to the periphery, leading to an accumulation of large numbers of vesicles and hence loss of lens transparency (PubMed:21636066).[1]
Function
FYCO1_HUMAN May mediate microtubule plus end-directed vesicle transport.[2]
References
- ↑ Chen J, Ma Z, Jiao X, Fariss R, Kantorow WL, Kantorow M, Pras E, Frydman M, Pras E, Riazuddin S, Riazuddin SA, Hejtmancik JF. Mutations in FYCO1 cause autosomal-recessive congenital cataracts. Am J Hum Genet. 2011 Jun 10;88(6):827-38. doi: 10.1016/j.ajhg.2011.05.008. PMID:21636066 doi:http://dx.doi.org/10.1016/j.ajhg.2011.05.008
- ↑ Pankiv S, Alemu EA, Brech A, Bruun JA, Lamark T, Overvatn A, Bjorkoy G, Johansen T. FYCO1 is a Rab7 effector that binds to LC3 and PI3P to mediate microtubule plus end-directed vesicle transport. J Cell Biol. 2010 Jan 25;188(2):253-69. PMID:20100911 doi:http://dx.doi.org/jcb.200907015
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