We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

6ejn

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

The KLC2 TPR domain bound to the JIP3 leucine zipper domain

Structural highlights

6ejn is a 4 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 3.2Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

KLC2_MOUSE Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends.[UniProtKB:Q9H0B6]

Publication Abstract from PubMed

Kinesin-1 transports numerous cellular cargoes along microtubules. The kinesin-1 light chain (KLC) mediates cargo binding and regulates kinesin-1 motility. To investigate the molecular basis for kinesin-1 recruitment and activation by cargoes, we solved the crystal structure of the KLC2 tetratricopeptide repeat (TPR) domain bound to the cargo JIP3. This, combined with biophysical and molecular evolutionary analyses, reveals a kinesin-1 cargo binding site, located on KLC TPR1, which is conserved in homologs from sponges to humans. In the complex, JIP3 crosslinks two KLC2 TPR domains via their TPR1s. We show that TPR1 forms a dimer interface that mimics JIP3 binding in all crystal structures of the unbound KLC TPR domain. We propose that cargo-induced dimerization of the KLC TPR domains via TPR1 is a general mechanism for activating kinesin-1. We relate this to activation by tryptophan-acidic cargoes, explaining how different cargoes activate kinesin-1 through related molecular mechanisms.

Insights into Kinesin-1 Activation from the Crystal Structure of KLC2 Bound to JIP3.,Cockburn JJB, Hesketh SJ, Mulhair P, Thomsen M, O'Connell MJ, Way M Structure. 2018 Aug 23. pii: S0969-2126(18)30257-0. doi:, 10.1016/j.str.2018.07.011. PMID:30197037^[1]

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

References

↑ Cockburn JJB, Hesketh SJ, Mulhair P, Thomsen M, O'Connell MJ, Way M. Insights into Kinesin-1 Activation from the Crystal Structure of KLC2 Bound to JIP3. Structure. 2018 Aug 23. pii: S0969-2126(18)30257-0. doi:, 10.1016/j.str.2018.07.011. PMID:30197037 doi:http://dx.doi.org/10.1016/j.str.2018.07.011

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/6ejn"

Categories: Large Structures | Mus musculus | Cockburn J | Hesketh SJ | Way M

@@ Line 1: / Line 1: @@
 ==The KLC2 TPR domain bound to the JIP3 leucine zipper domain==
-<StructureSection load='6ejn' size='340' side='right' caption='[[6ejn]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
+<StructureSection load='6ejn' size='340' side='right'caption='[[6ejn]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6ejn]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EJN FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6ejn]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EJN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EJN FirstGlance]. <br>
-</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">Klc2, mCG_8395 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice]), Mapk8ip3, Jip3, Jsap1, Syd2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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]] 3.2&#8491;</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=6ejn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ejn OCA], [http://pdbe.org/6ejn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ejn RCSB], [http://www.ebi.ac.uk/pdbsum/6ejn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ejn 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=6ejn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ejn OCA], [https://pdbe.org/6ejn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ejn RCSB], [https://www.ebi.ac.uk/pdbsum/6ejn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ejn ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/JIP3_MOUSE JIP3_MOUSE]] The JNK-interacting protein (JIP) group of scaffold proteins selectively mediates JNK signaling by aggregating specific components of the MAPK cascade to form a functional JNK signaling module. May function as a regulator of vesicle transport, through interactions with the JNK-signaling components and motor proteins.<ref>PMID:10523642</ref> <ref>PMID:10629060</ref>
+[https://www.uniprot.org/uniprot/KLC2_MOUSE KLC2_MOUSE] Kinesin is a microtubule-associated force-producing protein that plays a role in organelle transport. The light chain functions in coupling of cargo to the heavy chain or in the modulation of its ATPase activity. Through binding with PLEKHM2 and ARL8B, recruits kinesin-1 to lysosomes and hence direct lysosomes movement toward microtubule plus ends.[UniProtKB:Q9H0B6]
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 </div>
 <div class="pdbe-citations 6ejn" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Kinesin 3D Structures|Kinesin 3D Structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Lk3 transgenic mice]]
+[[Category: Large Structures]]
-[[Category: Cockburn, J]]
+[[Category: Mus musculus]]
-[[Category: Hesketh, S J]]
+[[Category: Cockburn J]]
-[[Category: Way, M]]
+[[Category: Hesketh SJ]]
-[[Category: Kinesin jip3 transport cargo molecular motor]]
+[[Category: Way M]]
-[[Category: Transport protein]]

6ejn

From Proteopedia

Current revision

The KLC2 TPR domain bound to the JIP3 leucine zipper domain

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