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4ejq

From Proteopedia

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Current revision

Crystal structure of KIF1A C-CC1-FHA

Structural highlights

4ejq is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.893Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

KIF1A_HUMAN Autosomal dominant nonsyndromic intellectual disability;Hereditary sensory and autonomic neuropathy type 2;Autosomal recessive spastic paraplegia type 30. The disease is caused by mutations affecting the gene represented in this entry.^[1] The disease is caused by mutations affecting the gene represented in this entry.^[2] The disease is caused by mutations affecting the gene represented in this entry.^[3]

Function

KIF1A_HUMAN Motor for anterograde axonal transport of synaptic vesicle precursors (By similarity).

Publication Abstract from PubMed

Kinesin-3 KIF1A plays prominent roles in axonal transport and synaptogenesis. KIF1A adopts a monomeric form in vitro but acts as a processive dimer in vivo. The mechanism underlying the motor dimerization is poorly understood. Here, we find that the CC1-FHA tandem of KIF1A exists as a stable dimer. The structure of CC1-FHA reveals that the linker between CC1 and FHA unexpectedly forms a beta-finger hairpin, which integrates CC1 with FHA assembling a CC1-FHA homodimer. More importantly, dissociation of the CC1-FHA dimer unleashes CC1 and the beta-finger, which are both essential for the motor inhibition. Thus, dimerization of the CC1-FHA tandem not only promotes the KIF1A dimer formation but also may trigger the motor activity via sequestering the CC1/beta-finger region. The CC1-FHA tandem likely functions as a hub for controlling the dimerization and activation of KIF1A, which may represent a new paradigm for the kinesin regulation shared by other kinesin-3 motors.

The CC1-FHA Tandem as a Central Hub for Controlling the Dimerization and Activation of Kinesin-3 KIF1A.,Huo L, Yue Y, Ren J, Yu J, Liu J, Yu Y, Ye F, Xu T, Zhang M, Feng W Structure. 2012 Sep 5;20(9):1550-61. Epub 2012 Aug 2. PMID:22863567^[4]

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

References

↑ Erlich Y, Edvardson S, Hodges E, Zenvirt S, Thekkat P, Shaag A, Dor T, Hannon GJ, Elpeleg O. Exome sequencing and disease-network analysis of a single family implicate a mutation in KIF1A in hereditary spastic paraparesis. Genome Res. 2011 May;21(5):658-64. doi: 10.1101/gr.117143.110. Epub 2011 Apr 12. PMID:21487076 doi:http://dx.doi.org/10.1101/gr.117143.110
↑ Riviere JB, Ramalingam S, Lavastre V, Shekarabi M, Holbert S, Lafontaine J, Srour M, Merner N, Rochefort D, Hince P, Gaudet R, Mes-Masson AM, Baets J, Houlden H, Brais B, Nicholson GA, Van Esch H, Nafissi S, De Jonghe P, Reilly MM, Timmerman V, Dion PA, Rouleau GA. KIF1A, an axonal transporter of synaptic vesicles, is mutated in hereditary sensory and autonomic neuropathy type 2. Am J Hum Genet. 2011 Aug 12;89(2):219-30. doi: 10.1016/j.ajhg.2011.06.013. Epub, 2011 Aug 4. PMID:21820098 doi:http://dx.doi.org/10.1016/j.ajhg.2011.06.013
↑ Hamdan FF, Gauthier J, Araki Y, Lin DT, Yoshizawa Y, Higashi K, Park AR, Spiegelman D, Dobrzeniecka S, Piton A, Tomitori H, Daoud H, Massicotte C, Henrion E, Diallo O, Shekarabi M, Marineau C, Shevell M, Maranda B, Mitchell G, Nadeau A, D'Anjou G, Vanasse M, Srour M, Lafreniere RG, Drapeau P, Lacaille JC, Kim E, Lee JR, Igarashi K, Huganir RL, Rouleau GA, Michaud JL. Excess of de novo deleterious mutations in genes associated with glutamatergic systems in nonsyndromic intellectual disability. Am J Hum Genet. 2011 Mar 11;88(3):306-16. doi: 10.1016/j.ajhg.2011.02.001. Epub, 2011 Mar 3. PMID:21376300 doi:10.1016/j.ajhg.2011.02.001
↑ Huo L, Yue Y, Ren J, Yu J, Liu J, Yu Y, Ye F, Xu T, Zhang M, Feng W. The CC1-FHA Tandem as a Central Hub for Controlling the Dimerization and Activation of Kinesin-3 KIF1A. Structure. 2012 Sep 5;20(9):1550-61. Epub 2012 Aug 2. PMID:22863567 doi:http://dx.doi.org/10.1016/j.str.2012.07.002

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/4ejq"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 4ejq is ON HOLD
+==Crystal structure of KIF1A C-CC1-FHA==
+<StructureSection load='4ejq' size='340' side='right'caption='[[4ejq]], [[Resolution|resolution]] 1.89&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4ejq]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EJQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4EJQ 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]] 1.893&#8491;</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=4ejq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ejq OCA], [https://pdbe.org/4ejq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4ejq RCSB], [https://www.ebi.ac.uk/pdbsum/4ejq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4ejq ProSAT]</span></td></tr>
+</table>
+== Disease ==
+[https://www.uniprot.org/uniprot/KIF1A_HUMAN KIF1A_HUMAN] Autosomal dominant nonsyndromic intellectual disability;Hereditary sensory and autonomic neuropathy type 2;Autosomal recessive spastic paraplegia type 30. The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:21487076</ref>   The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:21820098</ref>   The disease is caused by mutations affecting the gene represented in this entry.<ref>PMID:21376300</ref>
+== Function ==
+[https://www.uniprot.org/uniprot/KIF1A_HUMAN KIF1A_HUMAN] Motor for anterograde axonal transport of synaptic vesicle precursors (By similarity).
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Kinesin-3 KIF1A plays prominent roles in axonal transport and synaptogenesis. KIF1A adopts a monomeric form in vitro but acts as a processive dimer in vivo. The mechanism underlying the motor dimerization is poorly understood. Here, we find that the CC1-FHA tandem of KIF1A exists as a stable dimer. The structure of CC1-FHA reveals that the linker between CC1 and FHA unexpectedly forms a beta-finger hairpin, which integrates CC1 with FHA assembling a CC1-FHA homodimer. More importantly, dissociation of the CC1-FHA dimer unleashes CC1 and the beta-finger, which are both essential for the motor inhibition. Thus, dimerization of the CC1-FHA tandem not only promotes the KIF1A dimer formation but also may trigger the motor activity via sequestering the CC1/beta-finger region. The CC1-FHA tandem likely functions as a hub for controlling the dimerization and activation of KIF1A, which may represent a new paradigm for the kinesin regulation shared by other kinesin-3 motors.
-Authors: Huo,L, Yue,Y, Ren,J.Q, Yu,J, Liu,J.L, Yu,Y, Ye,F, Xu,T, Zhang,M.J, Feng,W
+The CC1-FHA Tandem as a Central Hub for Controlling the Dimerization and Activation of Kinesin-3 KIF1A.,Huo L, Yue Y, Ren J, Yu J, Liu J, Yu Y, Ye F, Xu T, Zhang M, Feng W Structure. 2012 Sep 5;20(9):1550-61. Epub 2012 Aug 2. PMID:22863567<ref>PMID:22863567</ref>
-Description: Crystal structure of KIF1A C-CC1-FHA
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4ejq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Kinesin 3D Structures|Kinesin 3D Structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Feng W]]
+[[Category: Huo L]]
+[[Category: Liu J]]
+[[Category: Ren J]]
+[[Category: Xu T]]
+[[Category: Ye F]]
+[[Category: Yu J]]
+[[Category: Yu Y]]
+[[Category: Yue Y]]
+[[Category: Zhang M]]

4ejq

From Proteopedia

Current revision

Crystal structure of KIF1A C-CC1-FHA

Structural highlights

Disease

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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