6a9x: Difference between revisions

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<StructureSection load='6a9x' size='340' side='right'caption='[[6a9x]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='6a9x' size='340' side='right'caption='[[6a9x]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[6a9x]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9X OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6A9X FirstGlance]. <br>
<table><tr><td colspan='2'>[[6a9x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6A9X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6A9X FirstGlance]. <br>
</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=6a9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9x OCA], [http://pdbe.org/6a9x PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6a9x RCSB], [http://www.ebi.ac.uk/pdbsum/6a9x PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9x ProSAT]</span></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]] 2.202&#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=6a9x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6a9x OCA], [https://pdbe.org/6a9x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6a9x RCSB], [https://www.ebi.ac.uk/pdbsum/6a9x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6a9x ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/GBRAP_MOUSE GBRAP_MOUSE]] Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity). [[http://www.uniprot.org/uniprot/ANK3_RAT ANK3_RAT]] Membrane-cytoskeleton linker. May participate in the maintenance/targeting of ion channels and cell adhesion molecules at the nodes of Ranvier and axonal initial segments. In skeletal muscle, required for costamere localization of DMD and betaDAG1 (By similarity). Regulates KCNA1 channel activity in function of dietary Mg(2+) levels, and thereby contributes to the regulation of renal Mg(2+) reabsorption (By similarity).[UniProtKB:G5E8K5]
[https://www.uniprot.org/uniprot/GBRAP_MOUSE GBRAP_MOUSE] Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity).
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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==See Also==
==See Also==
*[[Ankyrin 3D structures|Ankyrin 3D structures]]
*[[GABA receptor-associated protein 3D structures|GABA receptor-associated protein 3D structures]]
*[[GABA receptor-associated protein 3D structures|GABA receptor-associated protein 3D structures]]
== References ==
== References ==
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</StructureSection>
</StructureSection>
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Chen, K]]
[[Category: Mus musculus]]
[[Category: Li, J]]
[[Category: Rattus norvegicus]]
[[Category: Wang, C]]
[[Category: Chen K]]
[[Category: Zhang, M]]
[[Category: Li J]]
[[Category: Protein binding]]
[[Category: Wang C]]
[[Category: Signaling protein]]
[[Category: Zhang M]]
[[Category: Structural protein]]

Latest revision as of 12:21, 22 November 2023

Crystal Structure of AnkG/GABARAP ComplexCrystal Structure of AnkG/GABARAP Complex

Structural highlights

6a9x is a 2 chain structure with sequence from Mus musculus and Rattus norvegicus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.202Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GBRAP_MOUSE Ubiquitin-like modifier that plays a role in intracellular transport of GABA(A) receptors and its interaction with the cytoskeleton. Involved in apoptosis. Involved in autophagy. Whereas LC3s are involved in elongation of the phagophore membrane, the GABARAP/GATE-16 subfamily is essential for a later stage in autophagosome maturation (By similarity).

Publication Abstract from PubMed

GABAergic circuits are critical for the synchronization and higher order function of brain networks. Defects in this circuitry are linked to neuropsychiatric diseases, including bipolar disorder, schizophrenia, and autism. Work in cultured neurons has shown that ankyrin-G plays a key role in the regulation of GABAergic synapses on the axon initial segment and somatodendritic domain of pyramidal neurons, where it interacts directly with the GABAA receptor-associated protein (GABARAP) to stabilize cell surface GABAA receptors. Here, we generated a knock-in mouse model expressing a mutation that abolishes the ankyrin-G/GABARAP interaction (Ank3 W1989R) to understand how ankyrin-G and GABARAP regulate GABAergic circuitry in vivo. We found that Ank3 W1989R mice exhibit a striking reduction in forebrain GABAergic synapses resulting in pyramidal cell hyperexcitability and disruptions in network synchronization. In addition, we identified changes in pyramidal cell dendritic spines and axon initial segments consistent with compensation for hyperexcitability. Finally, we identified the ANK3 W1989R variant in a family with bipolar disorder, suggesting a potential role of this variant in disease. Our results highlight the importance of ankyrin-G in regulating forebrain circuitry and provide novel insights into how ANK3 loss-of-function variants may contribute to human disease.

Ankyrin-G regulates forebrain connectivity and network synchronization via interaction with GABARAP.,Nelson AD, Caballero-Floran RN, Rodriguez Diaz JC, Hull JM, Yuan Y, Li J, Chen K, Walder KK, Lopez-Santiago LF, Bennett V, McInnis MG, Isom LL, Wang C, Zhang M, Jones KS, Jenkins PM Mol Psychiatry. 2018 Nov 30. pii: 10.1038/s41380-018-0308-x. doi:, 10.1038/s41380-018-0308-x. PMID:30504823[1]

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

See Also

References

  1. Nelson AD, Caballero-Floran RN, Rodriguez Diaz JC, Hull JM, Yuan Y, Li J, Chen K, Walder KK, Lopez-Santiago LF, Bennett V, McInnis MG, Isom LL, Wang C, Zhang M, Jones KS, Jenkins PM. Ankyrin-G regulates forebrain connectivity and network synchronization via interaction with GABARAP. Mol Psychiatry. 2018 Nov 30. pii: 10.1038/s41380-018-0308-x. doi:, 10.1038/s41380-018-0308-x. PMID:30504823 doi:http://dx.doi.org/10.1038/s41380-018-0308-x

6a9x, resolution 2.20Å

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OCA