5jvr
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 5jvr is ON HOLD until Paper Publication Authors: Phillips, R.K., Rayment, I. Description: The neck-linker of Mus musculus KIF3A fused to the alpha ...) |
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The neck-linker of Mus musculus KIF3A fused to the alpha 7 helix of Drosophila melanogaster Kinesin-1 fused to EB1== |
| + | <StructureSection load='5jvr' size='340' side='right'caption='[[5jvr]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5jvr]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster], [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JVR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JVR FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=5jvr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jvr OCA], [https://pdbe.org/5jvr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jvr RCSB], [https://www.ebi.ac.uk/pdbsum/5jvr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jvr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/MARE1_HUMAN MARE1_HUMAN] Binds to the plus end of microtubules and regulates the dynamics of the microtubule cytoskeleton. Promotes cytoplasmic microtubule nucleation and elongation. May be involved in spindle function by stabilizing microtubules and anchoring them at centrosomes. May play a role in cell migration.<ref>PMID:12388762</ref> <ref>PMID:21646404</ref> <ref>PMID:16109370</ref> <ref>PMID:19632184</ref> [https://www.uniprot.org/uniprot/KIF3A_MOUSE KIF3A_MOUSE] Microtubule-based anterograde translocator for membranous organelles. Plus end-directed microtubule sliding activity in vitro. Plays a role in primary cilia formation.<ref>PMID:21670265</ref> [https://www.uniprot.org/uniprot/KINH_DROME KINH_DROME] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Kinesin-1, 2, 5, and 7 generate processive hand-over-hand 8-nm steps to transport intracellular cargoes toward the microtubule plus end. This processive motility requires gating mechanisms to coordinate the mechanochemical cycles of the two motor heads to sustain the processive run. A key structural element believed to regulate the degree of processivity is the neck-linker, a short peptide of 12-18 residues, which connects the motor domain to its coiled-coil stalk. While a shorter neck-linker has been correlated with longer run lengths, the structural data to support this hypothesis have been lacking. To test this hypothesis, seven kinesin structures were determined by X-ray crystallography. Each included the neck-linker motif, followed by helix alpha7 which constitutes the start of the coiled-coil stalk. In the majority of the structures, the neck-linker length differed from predictions because helix alpha7, which initiates the coiled-coil, started earlier in the sequence than predicted. A further examination of structures in the PDB reveals that there is a great disparity between the predicted and observed starting residues. This suggests that an accurate prediction of the start of a coiled-coil is currently difficult to achieve. These results are significant because they now exclude simple comparisons between members of the kinesin superfamily and add a further layer of complexity when interpreting the results of mutagenesis or protein fusion. They also re-emphasize the need to consider factors beyond the kinesin neck-linker motif when attempting to understand how inter-head communication is tuned to achieve the degree of processivity required for cellular function. | ||
| - | + | Family-specific kinesin structures reveal neck-linker length based on initiation of the coiled-coil.,Phillips RK, Peter LG, Gilbert SP, Rayment I J Biol Chem. 2016 Jul 26. pii: jbc.M116.737577. PMID:27462072<ref>PMID:27462072</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: Phillips | + | <div class="pdbe-citations 5jvr" style="background-color:#fffaf0;"></div> |
| - | [[Category: Rayment | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Drosophila melanogaster]] | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Mus musculus]] | ||
| + | [[Category: Phillips RK]] | ||
| + | [[Category: Rayment I]] | ||
Current revision
The neck-linker of Mus musculus KIF3A fused to the alpha 7 helix of Drosophila melanogaster Kinesin-1 fused to EB1
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