5i04: Difference between revisions

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'''Unreleased structure'''


The entry 5i04 is ON HOLD  until Paper Publication
==Crystal structure of the orphan region of human endoglin/CD105==
<StructureSection load='5i04' size='340' side='right' caption='[[5i04]], [[Resolution|resolution]] 2.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5i04]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5I04 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5I04 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=MAL:MALTOSE'>MAL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PGE:TRIETHYLENE+GLYCOL'>PGE</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5hzw|5hzw]], [[5hzv|5hzv]], [[5i05|5i05]]</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=5i04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5i04 OCA], [http://pdbe.org/5i04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5i04 RCSB], [http://www.ebi.ac.uk/pdbsum/5i04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5i04 ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/MALE_ECOLI MALE_ECOLI]] Involved in the high-affinity maltose membrane transport system MalEFGK. Initial receptor for the active transport of and chemotaxis toward maltooligosaccharides.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Endoglin (ENG)/CD105 is an essential endothelial cell co-receptor of the transforming growth factor beta (TGF-beta) superfamily, mutated in hereditary hemorrhagic telangiectasia type 1 (HHT1) and involved in tumor angiogenesis and preeclampsia. Here, we present crystal structures of the ectodomain of human ENG and its complex with the ligand bone morphogenetic protein 9 (BMP9). BMP9 interacts with a hydrophobic surface of the N-terminal orphan domain of ENG, which adopts a new duplicated fold generated by circular permutation. The interface involves residues mutated in HHT1 and overlaps with the epitope of tumor-suppressing anti-ENG monoclonal TRC105. The structure of the C-terminal zona pellucida module suggests how two copies of ENG embrace homodimeric BMP9, whose binding is compatible with ligand recognition by type I but not type II receptors. These findings shed light on the molecular basis of the BMP signaling cascade, with implications for future therapeutic interventions in this fundamental pathway.


Authors:  
Structural Basis of the Human Endoglin-BMP9 Interaction: Insights into BMP Signaling and HHT1.,Saito T, Bokhove M, Croci R, Zamora-Caballero S, Han L, Letarte M, de Sanctis D, Jovine L Cell Rep. 2017 May 30;19(9):1917-1928. doi: 10.1016/j.celrep.2017.05.011. PMID:28564608<ref>PMID:28564608</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 5i04" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bokhove, M]]
[[Category: Jovine, L]]
[[Category: Saito, T]]
[[Category: Sanctis, D de]]
[[Category: Angiogenesis]]
[[Category: Glycoprotein]]
[[Category: Orphan domain]]
[[Category: Receptor]]
[[Category: Signaling protein]]

Revision as of 10:23, 3 August 2017

Crystal structure of the orphan region of human endoglin/CD105

5i04, resolution 2.42Å

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