3gbw

<StructureSection load='3gbw' size='340' side='right' caption='[[3gbw]], [[Resolution|resolution]] 1.32&Aring;' scene=''>

<table><tr><td colspan='2'>[[3gbw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3GBW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3GBW FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=3gbw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gbw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3gbw RCSB], [http://www.ebi.ac.uk/pdbsum/3gbw PDBsum], [http://www.topsan.org/Proteins/NYSGXRC/3gbw TOPSAN]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/gb/3gbw_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

PHR [PAM (protein associated with Myc)-HIW (Highwire)-RPM-1 (regulator of presynaptic morphology 1)] proteins are conserved, large multi-domain E3 ubiquitin ligases with modular architecture. PHR proteins presynaptically control synaptic growth and axon guidance and postsynaptically regulate endocytosis of glutamate receptors. Dysfunction of neuronal ubiquitin-mediated proteasomal degradation is implicated in various neurodegenerative diseases. PHR proteins are characterized by the presence of two PHR domains near the N-terminus, which are essential for proper localization and function. Structures of both the first and second PHR domains of Mus musculus (mouse) Phr1 (MYC binding protein 2, Mycbp2) have been determined, revealing a novel beta sandwich fold composed of 11 antiparallel beta-strands. Conserved loops decorate the apical side of the first PHR domain (MmPHR1), yielding a distinct conserved surface feature. The surface of the second PHR domain (MmPHR2), in contrast, lacks significant conservation. Importantly, the structure of MmPHR1 provides insights into a loss-of-function mutation, Gly1092--&gt;Glu, observed in the Caenorhabditis elegans ortholog RPM-1.

Structures of PHR domains from Mus musculus Phr1 (Mycbp2) explain the loss-of-function mutation (Gly1092--&gt;Glu) of the C. elegans ortholog RPM-1.,Sampathkumar P, Ozyurt SA, Miller SA, Bain KT, Rutter ME, Gheyi T, Abrams B, Wang Y, Atwell S, Luz JG, Thompson DA, Wasserman SR, Emtage JS, Park EC, Rongo C, Jin Y, Klemke RL, Sauder JM, Burley SK J Mol Biol. 2010 Apr 9;397(4):883-92. Epub 2010 Feb 13. PMID:20156452<ref>PMID:20156452</ref>

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

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*[[Ubiquitin protein ligase|Ubiquitin protein ligase]]

[[Category: Klemke, R L]]

[[Category: Miller, S A]]

[[Category: Ozyurt, S A]]

[[Category: Tarun, G]]

[[Category: Myc-binding protein 2]]

[[Category: Mycbp2]]

[[Category: Nucleus]]

[[Category: Pam]]

[[Category: Phr domain]]

[[Category: Probable e3 ubiquitin-protein ligase mycbp2]]

[[Category: Protein associated with myc]]

[[Category: Ubl conjugation pathway]]

[[Category: Zinc-finger]]