5wde

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the KIFC3 motor domain in complex with ADP

Structural highlights

5wde is a 1 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 2h58. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.85Å
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KIFC3_HUMAN Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance.^[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

↑ Meng W, Mushika Y, Ichii T, Takeichi M. Anchorage of microtubule minus ends to adherens junctions regulates epithelial cell-cell contacts. Cell. 2008 Nov 28;135(5):948-59. doi: 10.1016/j.cell.2008.09.040. PMID:19041755 doi:http://dx.doi.org/10.1016/j.cell.2008.09.040
↑ 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 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

@@ Line 1: / Line 1: @@
 ==Crystal structure of the KIFC3 motor domain in complex with ADP==
-<StructureSection load='5wde' size='340' side='right' caption='[[5wde]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
+<StructureSection load='5wde' size='340' side='right'caption='[[5wde]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5wde]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2h58 2h58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WDE OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5WDE FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5wde]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=2h58 2h58]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WDE 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>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></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]] 1.85&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">KIFC3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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>, <scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</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=5wde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wde OCA], [http://pdbe.org/5wde PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wde RCSB], [http://www.ebi.ac.uk/pdbsum/5wde PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wde 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=5wde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wde OCA], [https://pdbe.org/5wde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wde RCSB], [https://www.ebi.ac.uk/pdbsum/5wde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wde ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/KIFC3_HUMAN KIFC3_HUMAN]] Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance.<ref>PMID:19041755</ref>
+[https://www.uniprot.org/uniprot/KIFC3_HUMAN KIFC3_HUMAN] Minus-end microtubule-dependent motor protein. Involved in apically targeted transport (By similarity). Required for zonula adherens maintenance.<ref>PMID:19041755</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5wde" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Kinesin 3D Structures|Kinesin 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
-[[Category: Arrowsmith, C H]]
+[[Category: Large Structures]]
-[[Category: Edwards, A M]]
+[[Category: Arrowsmith CH]]
-[[Category: Landry, R]]
+[[Category: Edwards AM]]
-[[Category: Park, H]]
+[[Category: Landry R]]
-[[Category: Structural genomic]]
+[[Category: Park H]]
-[[Category: Shen, Y]]
+[[Category: Shen Y]]
-[[Category: Tempel, W]]
+[[Category: Tempel W]]
-[[Category: Adp]]
-[[Category: Kinesin]]
-[[Category: Motor domain]]
-[[Category: Motor protein]]
-[[Category: Sgc]]

5wde

From Proteopedia

Current revision

Crystal structure of the KIFC3 motor domain in complex with ADP

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox