7azw

From Proteopedia

(Difference between revisions)

Current revision

Crystal structure of the MIZ1-BTB-domain

Structural highlights

7azw is a 2 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 2.1Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ZBT17_HUMAN Plays a critical role in early lymphocyte development, where it is essential to prevent apoptosis in lymphoid precursors, allowing them to survive in response to IL7 and undergo proper lineage commitment (By similarity). Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. Has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. Required for early embryonic development during gastrulation.^[1] ^[2] ^[3]

Publication Abstract from PubMed

The repurposing of structurally conserved protein domains in different functional contexts is thought to be a driving force in the evolution of complex protein interaction networks. The BTB/POZ domain is such a versatile binding module that occurs over 200 times in the human proteome with diverse protein-specific adaptations. In BTB-zinc-finger transcription factors, the BTB domain drives homo- and heterodimerization as well as interactions with non-BTB-domain-containing proteins. Which mechanisms encode specificity in these interactions at a structural level is incompletely understood. Here, we uncover an atypical peptide-binding site in the BTB domain of the MYC-interacting zinc-finger protein 1 (MIZ1) that arises from local flexibility of the core BTB fold and may provide a target site for MIZ1-directed therapeutic approaches. Intriguingly, the identified binding mode requires the BTB domain to be in a homodimeric state, thus holding opportunities for functional discrimination between homo- and heterodimers of MIZ1 in the cell.

Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1.,Orth B, Sander B, Moglich A, Diederichs K, Eilers M, Lorenz S Structure. 2021 Jun 22. pii: S0969-2126(21)00209-4. doi:, 10.1016/j.str.2021.06.005. PMID:34186024^[4]

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

References

↑ Peukert K, Staller P, Schneider A, Carmichael G, Hanel F, Eilers M. An alternative pathway for gene regulation by Myc. EMBO J. 1997 Sep 15;16(18):5672-86. PMID:9312026 doi:10.1093/emboj/16.18.5672
↑ Schneider A, Peukert K, Eilers M, Hanel F. Association of Myc with the zinc-finger protein Miz-1 defines a novel pathway for gene regulation by Myc. Curr Top Microbiol Immunol. 1997;224:137-46. PMID:9308237
↑ Basu S, Liu Q, Qiu Y, Dong F. Gfi-1 represses CDKN2B encoding p15INK4B through interaction with Miz-1. Proc Natl Acad Sci U S A. 2009 Feb 3;106(5):1433-8. doi: 10.1073/pnas.0804863106., Epub 2009 Jan 22. PMID:19164764 doi:10.1073/pnas.0804863106
↑ Orth B, Sander B, Moglich A, Diederichs K, Eilers M, Lorenz S. Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1. Structure. 2021 Jun 22. pii: S0969-2126(21)00209-4. doi:, 10.1016/j.str.2021.06.005. PMID:34186024 doi:http://dx.doi.org/10.1016/j.str.2021.06.005

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7azw"

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7azw is ON HOLD  until Paper Publication
+==Crystal structure of the MIZ1-BTB-domain==
+<StructureSection load='7azw' size='340' side='right'caption='[[7azw]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7azw]] is a 2 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=7AZW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AZW 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]] 2.1&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=7azw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7azw OCA], [https://pdbe.org/7azw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7azw RCSB], [https://www.ebi.ac.uk/pdbsum/7azw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7azw ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/ZBT17_HUMAN ZBT17_HUMAN] Plays a critical role in early lymphocyte development, where it is essential to prevent apoptosis in lymphoid precursors, allowing them to survive in response to IL7 and undergo proper lineage commitment (By similarity). Transcription factor that can function as an activator or repressor depending on its binding partners, and by targeting negative regulators of cell cycle progression. Has been shown to bind to the promoters of adenovirus major late protein and cyclin D1 and activate transcription. Required for early embryonic development during gastrulation.<ref>PMID:9312026</ref> <ref>PMID:9308237</ref> <ref>PMID:19164764</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The repurposing of structurally conserved protein domains in different functional contexts is thought to be a driving force in the evolution of complex protein interaction networks. The BTB/POZ domain is such a versatile binding module that occurs over 200 times in the human proteome with diverse protein-specific adaptations. In BTB-zinc-finger transcription factors, the BTB domain drives homo- and heterodimerization as well as interactions with non-BTB-domain-containing proteins. Which mechanisms encode specificity in these interactions at a structural level is incompletely understood. Here, we uncover an atypical peptide-binding site in the BTB domain of the MYC-interacting zinc-finger protein 1 (MIZ1) that arises from local flexibility of the core BTB fold and may provide a target site for MIZ1-directed therapeutic approaches. Intriguingly, the identified binding mode requires the BTB domain to be in a homodimeric state, thus holding opportunities for functional discrimination between homo- and heterodimers of MIZ1 in the cell.
-Authors:
+Identification of an atypical interaction site in the BTB domain of the MYC-interacting zinc-finger protein 1.,Orth B, Sander B, Moglich A, Diederichs K, Eilers M, Lorenz S Structure. 2021 Jun 22. pii: S0969-2126(21)00209-4. doi:, 10.1016/j.str.2021.06.005. PMID:34186024<ref>PMID:34186024</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 7azw" style="background-color:#fffaf0;"></div>
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Diederichs K]]
+[[Category: Lorenz S]]
+[[Category: Orth B]]
+[[Category: Sander B]]

7azw

From Proteopedia

Current revision

Crystal structure of the MIZ1-BTB-domain

Structural highlights

Function

Publication Abstract from PubMed

References

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Proteopedia Page Contributors and Editors (what is this?)

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