3hmk: Difference between revisions

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-{{Seed}}
-[[Image:3hmk.png|left|200px]]
-<!--
+==Crystal Structure of Serine Racemase==
-The line below this paragraph, containing "STRUCTURE_3hmk", creates the "Structure Box" on the page.
+<StructureSection load='3hmk' size='340' side='right'caption='[[3hmk]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[3hmk]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HMK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3HMK FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PLP:PYRIDOXAL-5-PHOSPHATE'>PLP</scene></td></tr>
-{{STRUCTURE_3hmk|  PDB=3hmk  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3hmk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3hmk OCA], [https://pdbe.org/3hmk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3hmk RCSB], [https://www.ebi.ac.uk/pdbsum/3hmk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3hmk ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SRR_RAT SRR_RAT] Catalyzes the synthesis of D-serine from L-serine. D-serine is a key coagonist with glutamate at NMDA receptors. Has dehydratase activity towards both L-serine and D-serine.<ref>PMID:16713567</ref> <ref>PMID:20106978</ref>
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/hm/3hmk_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </jmolCheckbox>
+</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/main_output.php?pdb_ID=3hmk ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Serine racemase is responsible for the synthesis of D-serine, an endogenous co-agonist for N-methyl-D-aspartate receptor-type glutamate receptors (NMDARs). This pyridoxal 5'-phosphate-dependent enzyme is involved both in the reversible conversion of L- to D-serine and serine catabolism by alpha,beta-elimination of water, thereby regulating D-serine levels. Because D-serine affects NMDAR signaling throughout the brain, serine racemase is a promising target for the treatment of disorders related to NMDAR dysfunction. To provide a molecular basis for rational drug design the x-ray crystal structures of human and rat serine racemase were determined at 1.5- and 2.1-A resolution, respectively, and in the presence and absence of the orthosteric inhibitor malonate. The structures revealed a fold typical of beta-family pyridoxal 5'-phosphate enzymes, with both a large domain and a flexible small domain associated into a symmetric dimer, and indicated a ligand-induced rearrangement of the small domain that organizes the active site for specific turnover of the substrate.
-===Crystal Structure of Serine Racemase===
+The structure of mammalian serine racemase: evidence for conformational changes upon inhibitor binding.,Smith MA, Mack V, Ebneth A, Moraes I, Felicetti B, Wood M, Schonfeld D, Mather O, Cesura A, Barker J J Biol Chem. 2010 Apr 23;285(17):12873-81. Epub 2010 Jan 27. PMID:20106978<ref>PMID:20106978</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_20106978}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 3hmk" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 20106978 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_20106978}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-HMK is a 2 chains structure with sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3HMK OCA].
-==Reference==
-<ref group="xtra">PMID:20106978</ref><references group="xtra"/>
 [[Category: Rattus norvegicus]]
-[[Category: Serine racemase]]
+[[Category: Barker J]]
-[[Category: Barker, J.]]
+[[Category: Ebneth A]]
-[[Category: Ebneth, A.]]
+[[Category: Felicetti B]]
-[[Category: Felicetti, B.]]
+[[Category: Mack V]]
-[[Category: Mack, V.]]
+[[Category: Smith MA]]
-[[Category: Smith, M A.]]
+[[Category: Woods M]]
-[[Category: Woods, M.]]
-[[Category: D-serine]]
-[[Category: Isomerase]]
-[[Category: Nmda glutamate receptor]]
-[[Category: Plp]]
-[[Category: Pyridoxal phosphate]]
-[[Category: Schizophrenia]]
-[[Category: Serine racemase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed May 12 10:28:56 2010''