8i3j
From Proteopedia
(Difference between revisions)
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8i3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i3j OCA], [https://pdbe.org/8i3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i3j RCSB], [https://www.ebi.ac.uk/pdbsum/8i3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i3j 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=8i3j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8i3j OCA], [https://pdbe.org/8i3j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8i3j RCSB], [https://www.ebi.ac.uk/pdbsum/8i3j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8i3j ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| - | == Disease == | ||
| - | [https://www.uniprot.org/uniprot/DYH1_HUMAN DYH1_HUMAN] Non-syndromic male infertility due to sperm motility disorder;Primary ciliary dyskinesia. The disease is caused by variants affecting the gene represented in this entry. The disease is caused by variants affecting the gene represented in this entry. | ||
| - | == Function == | ||
| - | [https://www.uniprot.org/uniprot/DYH1_HUMAN DYH1_HUMAN] Force generating protein of cilia required for sperm flagellum motility. Produces force towards the minus ends of microtubules. Dynein has ATPase activity; the force-producing power stroke is thought to occur on release of ADP. Required in spermatozoa for the formation of the inner dynein arms and biogenesis of the axoneme (PubMed:24360805).[UniProtKB:Q91XQ0]<ref>PMID:24360805</ref> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Axonemal dynein is an ATP-dependent microtubular motor protein responsible for cilia and flagella beating, and its dysfunction can cause diseases such as primary ciliary dyskinesia and sperm dysmotility. Despite its biological importance, structure-based mechanisms underlying axonemal dynein motors remain unclear. Here, we determined the X-ray crystal structure of the human inner-arm dynein-d (DNAH1) stalk region, which contains a long antiparallel coiled-coil and a microtubule-binding domain (MTBD), at 2.7 A resolution. Notably, differences in the relative orientation of the coiled-coil and MTBD in comparison with other dyneins, as well as the diverse orientations of the MTBD flap region among various isoforms, lead us to propose a 'spike shoe model' with an altered stepping angle for the interaction between IAD-d and microtubules. Based on these findings, we discuss isoform-specific functions of the axonemal dynein stalk MTBDs. | Axonemal dynein is an ATP-dependent microtubular motor protein responsible for cilia and flagella beating, and its dysfunction can cause diseases such as primary ciliary dyskinesia and sperm dysmotility. Despite its biological importance, structure-based mechanisms underlying axonemal dynein motors remain unclear. Here, we determined the X-ray crystal structure of the human inner-arm dynein-d (DNAH1) stalk region, which contains a long antiparallel coiled-coil and a microtubule-binding domain (MTBD), at 2.7 A resolution. Notably, differences in the relative orientation of the coiled-coil and MTBD in comparison with other dyneins, as well as the diverse orientations of the MTBD flap region among various isoforms, lead us to propose a 'spike shoe model' with an altered stepping angle for the interaction between IAD-d and microtubules. Based on these findings, we discuss isoform-specific functions of the axonemal dynein stalk MTBDs. | ||
| - | Crystal structure of the stalk region of axonemal inner-arm dynein-d reveals unique features in the coiled-coil and microtubule-binding domain.,Ko S, Toda A, Tanaka H, Yu J, Kurisu G FEBS Lett. 2023 | + | Crystal structure of the stalk region of axonemal inner-arm dynein-d reveals unique features in the coiled-coil and microtubule-binding domain.,Ko S, Toda A, Tanaka H, Yu J, Kurisu G FEBS Lett. 2023 Sep;597(17):2149-2160. doi: 10.1002/1873-3468.14690. Epub 2023 , Jul 3. PMID:37400274<ref>PMID:37400274</ref> |
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> | ||
Current revision
Crystal structure of human inner-arm dynein heavy chain d stalk and microtubule binding domain
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Categories: Homo sapiens | Large Structures | Ko S | Kurisu G | Tanaka H | Toda A | Yu J
