View source for 5ynr


==Solution Structure of glia maturation factor from Caenorhabditis elegans==
<StructureSection load='5ynr' size='340' side='right'caption='[[5ynr]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ynr]] 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=5YNR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YNR FirstGlance]. <br>
</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=5ynr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ynr OCA], [https://pdbe.org/5ynr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ynr RCSB], [https://www.ebi.ac.uk/pdbsum/5ynr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ynr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8IAA5_CAEEL Q8IAA5_CAEEL] 
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== Publication Abstract from PubMed ==
BACKGROUND: The GMF class of the ADF-H domain family proteins regulate actin dynamics by binding to the Arp2/3 complex and F-actin through their Site-1 and Site-2, respectively. CeGMF of C. elegans is analogous to GMFgamma of human and mouse and is 138 amino acids in length. METHODS: We have characterized the solution structure and dynamics of CeGMF by solution NMR spectroscopy and its thermal stability by DSC. RESULTS: The solution structure of CeGMF shows canonical ADF-H fold with two additional beta-strands in the beta4-beta5 loop region. The Site-1 of CeGMF is well formed and residues of all three regions of Site-1 show dynamic flexibility. However, the beta4-beta5 loop of Site-2 is less inclined towards the C-terminal, as the latter is truncated by four residues in comparison to GMF isoforms of human and mouse. Regions of Site-2 show motions on ns-ps timescale, but dynamic flexibility of beta4-beta5 loop is low in comparison to corresponding F-loop region of ADF/cofilin UNC-60B. A general difference in packing of alpha3 and alpha1 between GMF and ADF/cofilins was noticed. Additionally, thermal stability of CeGMF was significantly higher than its ADF/cofilin homologs. CONCLUSION: We have presented the first solution structure of GMF from C. elegans, which highlights the structural differences between the Site-2 of CeGMF and mammalian GMF isoforms. Further, we have seen the differences in structure, dynamics, and thermal stability of GMF and ADF/cofilin. GENERAL SIGNIFICANCE: This study provides a useful insight to structural and dynamics factors that define the specificity of GMF towards Arp2/3 complex.

Solution structure and dynamics of glia maturation factor from Caenorhabditis elegans.,Maheshwari D, Shukla VK, Jain A, Tripathi S, Kumar D, Arora A Biochim Biophys Acta Proteins Proteom. 2018 Jul 6;1866(10):1008-1020. doi:, 10.1016/j.bbapap.2018.06.007. PMID:29981887<ref>PMID:29981887</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5ynr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Caenorhabditis elegans]]
[[Category: Large Structures]]
[[Category: Arora A]]
[[Category: Kumar D]]
[[Category: Maheshwari D]]
[[Category: Shukla VK]]