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==Solution Structure of the PH Domain from the C. Elegans Muscle Protein UNC-89==
<StructureSection load='1fho' size='340' side='right'caption='[[1fho]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1fho]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Caenorhabditis_elegans Caenorhabditis elegans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FHO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FHO FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1fho FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fho OCA], [https://pdbe.org/1fho PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fho RCSB], [https://www.ebi.ac.uk/pdbsum/1fho PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fho ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/UNC89_CAEEL UNC89_CAEEL] Structural component of the muscle M-line. Myofilament lattice assembly begins with positional cues laid down in the basement membrane and muscle cell membrane. UNC-89 responds to these signals, localizes, and then participates in assembling an M-line.<ref>PMID:8603916</ref> <ref>PMID:15313609</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
BACKGROUND: Pleckstrin homology (PH) domains constitute a structurally conserved family present in many signaling and regulatory proteins. PH domains have been shown to bind to phospholipids, and many function in membrane targeting. They generally have a strong electrostatic polarization and interact with negatively charged phospholipids via the positive pole. On the basis of electrostatic modeling, however, we have previously identified a class of PH domains with a predominantly negative charge and predicted that these domains recognize other targets. Here, we report the first experimental structure of such a PH domain. RESULTS: The structure of the PH domain from Caenorhabditis elegans muscle protein UNC-89 has been determined by heteronuclear NMR. The domain adopts the classic PH fold, but has an unusual closed conformation of the "inositol binding loops. This creates a small opening to a deep hydrophobic pocket lined with negative charges on one side, and provides a molecular explanation for the lack of association with inositol-1,4,5-triphosphate. As predicted, the PH domain of UNC-89 has a strongly negative overall electrostatic potential. Modeling the Dbl homology (DH)-linked PH domains from the C. elegans genome shows that a large proportion of these modules are negatively charged. CONCLUSIONS: We present the first structure of a PH domain with a strong negative overall electrostatic potential. The presence of a deep pocket lined with negative charges suggests that the domain binds to ligands other than acidic phospholipids. The abundance of this class of PH domain in the C. elegans genome suggests a prominent role in mediating protein-protein interactions.

Structure of a PH domain from the C. elegans muscle protein UNC-89 suggests a novel function.,Blomberg N, Baraldi E, Sattler M, Saraste M, Nilges M Structure. 2000 Oct 15;8(10):1079-87. PMID:11080629<ref>PMID:11080629</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fho" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Baraldi E]]
[[Category: Blomberg N]]
[[Category: Nilges M]]
[[Category: Saraste M]]
[[Category: Sattler M]]