9c1b: Difference between revisions

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'''Unreleased structure'''


The entry 9c1b is ON HOLD  until 2026-05-28
==Crystal structure of GDP-bound human M-RAS protein in crystal form II==
<StructureSection load='9c1b' size='340' side='right'caption='[[9c1b]], [[Resolution|resolution]] 2.27&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9c1b]] is a 4 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=9C1B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9C1B 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]] 2.27&#8491;</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=9c1b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9c1b OCA], [https://pdbe.org/9c1b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9c1b RCSB], [https://www.ebi.ac.uk/pdbsum/9c1b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9c1b ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/RASM_HUMAN RASM_HUMAN] Noonan syndrome. The disease is caused by variants affecting the gene represented in this entry.
== Function ==
[https://www.uniprot.org/uniprot/RASM_HUMAN RASM_HUMAN] Serves as an important signal transducer for a novel upstream stimuli in controlling cell proliferation. Activates the MAP kinase pathway.<ref>PMID:16630891</ref> <ref>PMID:28289718</ref>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
M-RAS plays a crucial role in the RAF-MEK signaling pathway. When activated by GTP, M-RAS forms a complex with SHOC2 and PP1C, initiating downstream RAF-MEK signal transduction. In this study, the crystal structure of the GDP-bound human M-RAS protein is presented with two forms of crystal packing. Both the full-length and truncated human M-RAS structures aligned well with the high-confidence section of the AlphaFold2-predicted structure with low r.m.s.d., except for the Switch regions. Despite high sequence similarity to the available mouse M-RAS structure, the full-length human M-RAS structure exhibits unique crystal packing. This inactive human M-RAS structure could offer novel insights for the design of selective compounds targeting M-RAS.


Authors:  
Crystal structure of the GDP-bound human M-RAS protein in two crystal forms.,Bester SM, Abrahamsen R, Rodrigues Samora L, Wu WI, Mou TC Acta Crystallogr F Struct Biol Commun. 2024 Sep 1;80(Pt 9):220-227. doi: , 10.1107/S2053230X24007969. Epub 2024 Aug 28. PMID:39196705<ref>PMID:39196705</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 9c1b" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Abrahamsen R]]
[[Category: Bester SM]]
[[Category: Mou T-C]]
[[Category: Samora LR]]
[[Category: Wu W-I]]
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