6cmy: Difference between revisions

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~~'''Unreleased structure'''~~

~~The~~ entry 6cmy is ~~ON HOLD until Paper Publication~~

==Solution NMR Structure Determination of Mouse Melanoregulin==

== Structural highlights ==

<table><tr><td colspan='2'>[[6cmy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5kbo 5kbo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CMY 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=6cmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cmy OCA], [https://pdbe.org/6cmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cmy RCSB], [https://www.ebi.ac.uk/pdbsum/6cmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cmy ProSAT]</span></td></tr>

</table>

== Function ==

[https://www.uniprot.org/uniprot/MREG_MOUSE MREG_MOUSE] Plays a role in the incorporation of pigments into hair. May function in membrane fusion and regulate the biogenesis of disk membranes of photoreceptor rod cells.<ref>PMID:15550542</ref> <ref>PMID:17260955</ref>

== Publication Abstract from PubMed ==

Melanoregulin (Mreg) is a small, highly charged, multiply palmitoylated protein present on the membrane of melanosomes. Mreg is implicated in the transfer of melanosomes from melanocytes to keratinocytes, and in promoting the microtubule minus end-directed transport of these organelles. The possible molecular function of Mreg was identified by solving its structure using nuclear magnetic resonance (NMR) spectroscopy. Mreg contains six alpha helices forming a fishhook-like fold in which positive and negative charges occupy opposite sides of the protein's surface and sandwich a putative, cholesterol recognition sequence (CRAC motif). Mreg containing a point mutation within its CRAC motif still targets to late endosomes/lysosomes, but no longer promotes their microtubule minus end-directed transport. Moreover, wild-type Mreg does not promote the microtubule minus end-directed transport of late endosomes/lysosomes in cells transiently depleted of cholesterol. Finally, reversing the charge of three clustered acidic residues partially inhibits Mreg's ability to drive these organelles to microtubule minus ends.

~~Authors:~~ Rout~~, A.K.~~, Wu, X., Strub, M.P., ~~Starich, M~~.R.~~, Hammer III, J~~.A.~~, Tjandra, N~~.

The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function.,Rout AK, Wu X, Starich MR, Strub MP, Hammer JA, Tjandra N Structure. 2018 Aug 8. pii: S0969-2126(18)30255-7. doi:, 10.1016/j.str.2018.07.009. PMID:30174147<ref>PMID:30174147</ref>

~~Description~~: ~~Solution NMR Structure Determination of Mouse Melanoregulin~~

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>

[[Category: ~~Unreleased~~ Structures]]

</div>

[[Category: ~~Wu, X~~]]

[[Category: ~~Starich, M.R~~]]

== References ==

[[Category: ~~Hammer Iii, J.A~~]]

[[Category: ~~Tjandra, N~~]]

__TOC__

[[Category: ~~Rout, A.K~~]]

</StructureSection>

[[Category: ~~Strub, M.P~~]]

[[Category: Large Structures]]

[[Category: Mus musculus]]

[[Category: Hammer III JA]]

[[Category: Rout AK]]

[[Category: Starich MR]]

[[Category: Strub MP]]

[[Category: Tjandra N]]

[[Category: Wu X]]

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@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 6cmy is ON HOLD  until Paper Publication
+==Solution NMR Structure Determination of Mouse Melanoregulin==
+<StructureSection load='6cmy' size='340' side='right'caption='[[6cmy]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[6cmy]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=5kbo 5kbo]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6CMY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6CMY 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=6cmy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6cmy OCA], [https://pdbe.org/6cmy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6cmy RCSB], [https://www.ebi.ac.uk/pdbsum/6cmy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6cmy ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/MREG_MOUSE MREG_MOUSE] Plays a role in the incorporation of pigments into hair. May function in membrane fusion and regulate the biogenesis of disk membranes of photoreceptor rod cells.<ref>PMID:15550542</ref> <ref>PMID:17260955</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Melanoregulin (Mreg) is a small, highly charged, multiply palmitoylated protein present on the membrane of melanosomes. Mreg is implicated in the transfer of melanosomes from melanocytes to keratinocytes, and in promoting the microtubule minus end-directed transport of these organelles. The possible molecular function of Mreg was identified by solving its structure using nuclear magnetic resonance (NMR) spectroscopy. Mreg contains six alpha helices forming a fishhook-like fold in which positive and negative charges occupy opposite sides of the protein's surface and sandwich a putative, cholesterol recognition sequence (CRAC motif). Mreg containing a point mutation within its CRAC motif still targets to late endosomes/lysosomes, but no longer promotes their microtubule minus end-directed transport. Moreover, wild-type Mreg does not promote the microtubule minus end-directed transport of late endosomes/lysosomes in cells transiently depleted of cholesterol. Finally, reversing the charge of three clustered acidic residues partially inhibits Mreg's ability to drive these organelles to microtubule minus ends.
-Authors: Rout, A.K., Wu, X., Strub, M.P., Starich, M.R., Hammer III, J.A., Tjandra, N.
+The Structure of Melanoregulin Reveals a Role for Cholesterol Recognition in the Protein's Ability to Promote Dynein Function.,Rout AK, Wu X, Starich MR, Strub MP, Hammer JA, Tjandra N Structure. 2018 Aug 8. pii: S0969-2126(18)30255-7. doi:, 10.1016/j.str.2018.07.009. PMID:30174147<ref>PMID:30174147</ref>
-Description: Solution NMR Structure Determination of Mouse Melanoregulin
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Wu, X]]
+<div class="pdbe-citations 6cmy" style="background-color:#fffaf0;"></div>
-[[Category: Starich, M.R]]
+== References ==
-[[Category: Hammer Iii, J.A]]
+<references/>
-[[Category: Tjandra, N]]
+__TOC__
-[[Category: Rout, A.K]]
+</StructureSection>
-[[Category: Strub, M.P]]
+[[Category: Large Structures]]
+[[Category: Mus musculus]]
+[[Category: Hammer III JA]]
+[[Category: Rout AK]]
+[[Category: Starich MR]]
+[[Category: Strub MP]]
+[[Category: Tjandra N]]
+[[Category: Wu X]]