This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

5w3d

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 08:47, 30 September 2020

The structure of kinesin-14 wild-type Ncd-ADP dimer

Structural highlights

5w3d is a 2 chain structure. 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

Function

[NCD_DROME] NCD is required for normal chromosomal segregation in meiosis, in females, and in early mitotic divisions of the embryo. The NCD motor activity is directed toward the microtubule's minus end.^[1]

Publication Abstract from PubMed

Kinesin microtubule motor proteins play essential roles in division, including attaching chromosomes to spindles and crosslinking microtubules for spindle assembly. Human kinesin-14 KIFC1 is unique in that cancer cells with amplified centrosomes are dependent on the motor for viable division because of its ability to cluster centrosomes and form bipolar spindles, but it is not required for division in almost all normal cells. Screens for small molecule inhibitors of KIFC1 have yielded several candidates for further development, but obtaining structural data to determine their sites of binding has been difficult. Here we compare a previously unreported KIFC1 crystal structure with new structures of two closely related kinesin-14 proteins, Ncd and KIFC3, to determine the potential binding site of a known KIFC1 ATPase inhibitor, AZ82. We analyze the previously identified kinesin inhibitor binding sites and identify features of AZ82 that favor binding to one of the sites, the alpha4/alpha6 site. This selectivity can be explained by unique structural features of the KIFC1 alpha4/alpha6 binding site. These features may help improve the drug-like properties of AZ82 and other specific KIFC1 inhibitors.

Structural basis of small molecule ATPase inhibition of a human mitotic kinesin motor protein.,Park HW, Ma Z, Zhu H, Jiang S, Robinson RC, Endow SA Sci Rep. 2017 Nov 9;7(1):15121. doi: 10.1038/s41598-017-14754-6. PMID:29123223^[2]

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

References

↑ Walker RA, Salmon ED, Endow SA. The Drosophila claret segregation protein is a minus-end directed motor molecule. Nature. 1990 Oct 25;347(6295):780-2. PMID:2146510 doi:http://dx.doi.org/10.1038/347780a0
↑ Park HW, Ma Z, Zhu H, Jiang S, Robinson RC, Endow SA. Structural basis of small molecule ATPase inhibition of a human mitotic kinesin motor protein. Sci Rep. 2017 Nov 9;7(1):15121. doi: 10.1038/s41598-017-14754-6. PMID:29123223 doi:http://dx.doi.org/10.1038/s41598-017-14754-6

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5w3d"

@@ Line 1: / Line 1: @@
 ==The structure of kinesin-14 wild-type Ncd-ADP dimer==
-<StructureSection load='5w3d' size='340' side='right' caption='[[5w3d]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
+<StructureSection load='5w3d' size='340' side='right'caption='[[5w3d]], [[Resolution|resolution]] 2.79&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5w3d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W3D OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5W3D FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5w3d]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5W3D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5W3D 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=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=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=5w3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w3d OCA], [http://pdbe.org/5w3d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w3d RCSB], [http://www.ebi.ac.uk/pdbsum/5w3d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w3d ProSAT]</span></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=5w3d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5w3d OCA], [http://pdbe.org/5w3d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5w3d RCSB], [http://www.ebi.ac.uk/pdbsum/5w3d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5w3d ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 22: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Large Structures]]
 [[Category: Chacko, J]]
 [[Category: Endow, S A]]

5w3d

From Proteopedia

Revision as of 08:47, 30 September 2020

The structure of kinesin-14 wild-type Ncd-ADP dimer

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox