4rh7

From Proteopedia

(Difference between revisions)

Revision as of 06:56, 2 March 2023

Crystal structure of human cytoplasmic dynein 2 motor domain in complex with ADP.Vi

Structural highlights

4rh7 is a 1 chain structure with sequence from Homo sapiens and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, , ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

DYHC2_HUMAN Short rib-polydactyly syndrome, Majewski type;Short rib-polydactyly syndrome, Saldino-Noonan type;Jeune syndrome;Short rib-polydactyly syndrome, Verma-Naumoff type. The disease is caused by variants affecting the gene represented in this entry. In some cases DYNC2H1 mutations result in disease phenotype in the presence of mutations in NEK1 indicating digenic inheritance (digenic short rib-polydactyly syndrome 3/6 with polydactyly) (PubMed:21211617).^[1]

Function

DYHC2_HUMAN May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis. May play a role in transport between endoplasmic reticulum and Golgi or organization of the Golgi in cells (By similarity).

Publication Abstract from PubMed

Members of the dynein family, consisting of cytoplasmic and axonemal isoforms, are motors that move towards the minus ends of microtubules. Cytoplasmic dynein-1 (dynein-1) plays roles in mitosis and cellular cargo transport, and is implicated in viral infections and neurodegenerative diseases. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Here we present the crystal structure of the human cytoplasmic dynein-2 motor bound to the ATP-hydrolysis transition state analogue ADP.vanadate. The structure reveals a closure of the motor's ring of six AAA+ domains (ATPases associated with various cellular activites: AAA1-AAA6). This induces a steric clash with the linker, the key element for the generation of movement, driving it into a conformation that is primed to produce force. Ring closure also changes the interface between the stalk and buttress coiled-coil extensions of the motor domain. This drives helix sliding in the stalk which causes the microtubule binding domain at its tip to release from the microtubule. Our structure answers the key questions of how ATP hydrolysis leads to linker remodelling and microtubule affinity regulation.

Structure of human cytoplasmic dynein-2 primed for its power stroke.,Schmidt H, Zalyte R, Urnavicius L, Carter AP Nature. 2014 Dec 1. doi: 10.1038/nature14023. PMID:25470043^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Thiel C, Kessler K, Giessl A, Dimmler A, Shalev SA, von der Haar S, Zenker M, Zahnleiter D, Stoss H, Beinder E, Abou Jamra R, Ekici AB, Schroder-Kress N, Aigner T, Kirchner T, Reis A, Brandstatter JH, Rauch A. NEK1 mutations cause short-rib polydactyly syndrome type majewski. Am J Hum Genet. 2011 Jan 7;88(1):106-14. doi: 10.1016/j.ajhg.2010.12.004. PMID:21211617 doi:http://dx.doi.org/10.1016/j.ajhg.2010.12.004
↑ Schmidt H, Zalyte R, Urnavicius L, Carter AP. Structure of human cytoplasmic dynein-2 primed for its power stroke. Nature. 2014 Dec 1. doi: 10.1038/nature14023. PMID:25470043 doi:http://dx.doi.org/10.1038/nature14023

1 Structural highlights
2 Disease
3 Function
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4rh7"

@@ Line 3: / Line 3: @@
 <StructureSection load='4rh7' size='340' side='right'caption='[[4rh7]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[4rh7]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Synthetic_construct_sequences Synthetic construct sequences]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RH7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4RH7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[4rh7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4RH7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4RH7 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AOV:ADP+ORTHOVANADATE'>AOV</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=AOV:ADP+ORTHOVANADATE'>AOV</scene>, <scene name='pdbligand=ATP:ADENOSINE-5-TRIPHOSPHATE'>ATP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=4rh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rh7 OCA], [http://pdbe.org/4rh7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4rh7 RCSB], [http://www.ebi.ac.uk/pdbsum/4rh7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4rh7 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=4rh7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4rh7 OCA], [https://pdbe.org/4rh7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4rh7 RCSB], [https://www.ebi.ac.uk/pdbsum/4rh7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4rh7 ProSAT]</span></td></tr>
 </table>
+== Disease ==
+[https://www.uniprot.org/uniprot/DYHC2_HUMAN DYHC2_HUMAN] Short rib-polydactyly syndrome, Majewski type;Short rib-polydactyly syndrome, Saldino-Noonan type;Jeune syndrome;Short rib-polydactyly syndrome, Verma-Naumoff type. The disease is caused by variants affecting the gene represented in this entry. In some cases DYNC2H1 mutations result in disease phenotype in the presence of mutations in NEK1 indicating digenic inheritance (digenic short rib-polydactyly syndrome 3/6 with polydactyly) (PubMed:21211617).<ref>PMID:21211617</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/DYHC2_HUMAN DYHC2_HUMAN] May function as a motor for intraflagellar retrograde transport. Functions in cilia biogenesis. May play a role in transport between endoplasmic reticulum and Golgi or organization of the Golgi in cells (By similarity).
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 24: / Line 28: @@
 __TOC__
 </StructureSection>
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Synthetic construct sequences]]
+[[Category: Synthetic construct]]
-[[Category: Carter, A P]]
+[[Category: Carter AP]]
-[[Category: Schmidt, H]]
+[[Category: Schmidt H]]
-[[Category: Urnavicius, L]]
+[[Category: Urnavicius L]]
-[[Category: Zalyte, R]]
+[[Category: Zalyte R]]
-[[Category: Aaa+ protein]]
-[[Category: Dynein motor domain]]
-[[Category: Motor protein]]

4rh7

From Proteopedia

Revision as of 06:56, 2 March 2023

Crystal structure of human cytoplasmic dynein 2 motor domain in complex with ADP.Vi

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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