7l0j

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(New page: '''Unreleased structure''' The entry 7l0j is ON HOLD until Paper Publication Authors: Description: Category: Unreleased Structures)
Current revision (15:35, 18 October 2023) (edit) (undo)
 
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'''Unreleased structure'''
 
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The entry 7l0j is ON HOLD until Paper Publication
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==Structure of AMH bound to AMHR2-ECD==
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<StructureSection load='7l0j' size='340' side='right'caption='[[7l0j]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[7l0j]] 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=7L0J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7L0J FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=7l0j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7l0j OCA], [https://pdbe.org/7l0j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7l0j RCSB], [https://www.ebi.ac.uk/pdbsum/7l0j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7l0j ProSAT]</span></td></tr>
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</table>
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== Disease ==
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[https://www.uniprot.org/uniprot/MIS_HUMAN MIS_HUMAN] Persistent Muellerian duct syndrome. The disease is caused by variants affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/MIS_HUMAN MIS_HUMAN] Plays an important role in several reproductive functions. Induces Muellerian duct regression during male fetal sexual differentiation (PubMed:3754790, PubMed:34155118, PubMed:8469238). Also plays a role in Leydig cell differentiation and function (By similarity). In female acts as a negative regulator of the primordial to primary follicle transition and decreases FSH sensitivity of growing follicles (PubMed:14742691). AMH signals by binding to a specific type-II receptor, AMHR2, that heterodimerizes with type-I receptors (ACVR1 and BMPR1A), and recruiting SMAD proteins that are translocated to the nucleus to regulate target gene expression (PubMed:20861221, PubMed:34155118).[UniProtKB:P27106]<ref>PMID:14742691</ref> <ref>PMID:20861221</ref> <ref>PMID:34155118</ref> <ref>PMID:3754790</ref> <ref>PMID:8469238</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Anti-Mullerian hormone (AMH), or Mullerian-inhibiting substance, is a protein hormone that promotes Mullerian duct regression during male fetal sexual differentiation and regulation of folliculogenesis in women. AMH is a member of the transforming growth factor beta (TGF-beta) family, which has evolved to signal through its own dedicated type II receptor, AMH receptor type II (AMHR2). Structures of other TGF-beta family members have revealed how ligands infer specificity for their cognate receptors; however, it is unknown how AMH binds AMHR2 at the molecular level. Therefore, in this study, we solved the X-ray crystal structure of AMH bound to the extracellular domain of AMHR2 to a resolution of 2.6A. The structure reveals that while AMH binds AMHR2 in a similar location to Activin and BMP ligand binding to their type II receptors, differences in both AMH and AMHR2 account for a highly specific interaction. Furthermore, using an AMH responsive cell-based luciferase assay, we show that a conformation in finger 1 of AMHR2 and a salt bridge formed by K534 on AMH and D81/E84 of AMHR2 are key to the AMH/AMHR2 interaction. Overall, our study highlights how AMH engages AMHR2 using a modified paradigm of receptor binding facilitated by modifications to the three-finger toxin fold of AMHR2. Furthermore, understanding these elements contributing to the specificity of binding will help in the design of agonists or antagonists or the selection of antibody therapies.
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Authors:
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Structure of AMH bound to AMHR2 provides insight into a unique signaling pair in the TGF-beta family.,Hart KN, Stocker WA, Nagykery NG, Walton KL, Harrison CA, Donahoe PK, Pepin D, Thompson TB Proc Natl Acad Sci U S A. 2021 Jun 29;118(26):e2104809118. doi: , 10.1073/pnas.2104809118. PMID:34155118<ref>PMID:34155118</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 7l0j" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Homo sapiens]]
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[[Category: Large Structures]]
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[[Category: Hart KN]]
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[[Category: Thompson TB]]

Current revision

Structure of AMH bound to AMHR2-ECD

PDB ID 7l0j

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