2ga2

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[[Image:2ga2.jpg|left|200px]]
 
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==h-MetAP2 complexed with A193400==
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The line below this paragraph, containing "STRUCTURE_2ga2", creates the "Structure Box" on the page.
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<StructureSection load='2ga2' size='340' side='right'caption='[[2ga2]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2ga2]] is a 1 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=2GA2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2GA2 FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.95&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A19:5-BROMO-2-{[(4-CHLOROPHENYL)SULFONYL]AMINO}BENZOIC+ACID'>A19</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
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{{STRUCTURE_2ga2| PDB=2ga2 | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ga2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ga2 OCA], [https://pdbe.org/2ga2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ga2 RCSB], [https://www.ebi.ac.uk/pdbsum/2ga2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ga2 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/MAP2_HUMAN MAP2_HUMAN] Cotranslationally removes the N-terminal methionine from nascent proteins. The N-terminal methionine is often cleaved when the second residue in the primary sequence is small and uncharged (Met-Ala-, Cys, Gly, Pro, Ser, Thr, or Val). The catalytic activity of human METAP2 toward Met-Val peptides is consistently two orders of magnitude higher than that of METAP1, suggesting that it is responsible for processing proteins containing N-terminal Met-Val and Met-Thr sequences in vivo. Protects eukaryotic initiation factor EIF2S1 from translation-inhibiting phosphorylation by inhibitory kinases such as EIF2AK2/PKR and EIF2AK1/HCR. Plays a critical role in the regulation of protein synthesis.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ga/2ga2_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2ga2 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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We have screened molecules for inhibition of MetAP2 as a novel approach toward antiangiogenesis and anticancer therapy using affinity selection/mass spectrometry (ASMS) employing MetAP2 loaded with Mn(2+) as the active site metal. After a series of anthranilic acid sulfonamides with micromolar affinities was identified, chemistry efforts were initiated. The micromolar hits were quickly improved to potent nanomolar inhibitors by chemical modifications guided by insights from X-ray crystallography.
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'''h-MetAP2 complexed with A193400'''
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Development of sulfonamide compounds as potent methionine aminopeptidase type II inhibitors with antiproliferative properties.,Kawai M, BaMaung NY, Fidanze SD, Erickson SA, Tedrow JS, Sanders WJ, Vasudevan A, Park C, Hutchins C, Comess KM, Kalvin D, Wang J, Zhang Q, Lou P, Tucker-Garcia L, Bouska J, Bell RL, Lesniewski R, Henkin J, Sheppard GS Bioorg Med Chem Lett. 2006 Jul 1;16(13):3574-7. Epub 2006 May 2. PMID:16632353<ref>PMID:16632353</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2ga2" style="background-color:#fffaf0;"></div>
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==About this Structure==
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==See Also==
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2GA2 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2GA2 OCA].
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*[[Aminopeptidase 3D structures|Aminopeptidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Methionyl aminopeptidase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Park C]]
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[[Category: Park, C H.]]
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[[Category: Complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:52:22 2008''
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Current revision

h-MetAP2 complexed with A193400

PDB ID 2ga2

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