4cd1
From Proteopedia
(Difference between revisions)
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4cd1]] is a 1 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=4CD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CD1 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4cd1]] is a 1 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=4CD1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4CD1 FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8E9:1-AMINO-4-(3-METHYLPHENYL)AMINO-9,10-DIOXO-9,10-DIHYDROANTHRACENE-2-SULFONATE'>8E9</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=8E9:1-AMINO-4-(3-METHYLPHENYL)AMINO-9,10-DIOXO-9,10-DIHYDROANTHRACENE-2-SULFONATE'>8E9</scene></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=4cd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cd1 OCA], [https://pdbe.org/4cd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cd1 RCSB], [https://www.ebi.ac.uk/pdbsum/4cd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cd1 ProSAT]</span></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=4cd1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4cd1 OCA], [https://pdbe.org/4cd1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4cd1 RCSB], [https://www.ebi.ac.uk/pdbsum/4cd1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4cd1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [https://www.uniprot.org/uniprot/ENTP2_RAT ENTP2_RAT] In the nervous system, could hydrolyze ATP and other nucleotides to regulate purinergic neurotransmission. Hydrolyzes ADP only to a marginal extent. | |
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | In many vertebrate tissues CD39-like ecto-nucleoside triphosphate diphosphohydrolases (NTPDases) act in concert with ecto-5'-nucleotidase (e5NT, CD73) to convert extracellular ATP to adenosine. Extracellular ATP is a cytotoxic, pro-inflammatory signalling molecule whereas its product adenosine constitutes a universal and potent immune suppressor. Interference with these ectonucleotidases by use of small molecule inhibitors or inhibitory antibodies appears to be an effective strategy to enhance anti-tumour immunity and suppress neoangiogenesis. Here we present the first crystal structures of an NTPDase catalytic ectodomain in complex with the Reactive Blue 2 (RB2)-derived inhibitor PSB-071. In both of the two crystal forms presented the inhibitor binds as a sandwich of two molecules at the nucleoside binding site. One of the molecules is well defined in its orientation. Specific hydrogen bonds are formed between the sulfonyl group and the nucleoside binding loop. The methylphenyl side chain functionality that improved NTPDase2-specificity is sandwiched between R245 and R394, the latter of which is exclusively found in NTPDase2. The second molecule exhibits great in-plane rotational freedom and could not be modelled in a specific orientation. In addition to this structural insight into NTPDase inhibition, the observation of the putative membrane interaction loop (MIL) in two different conformations related by a 10 degrees rotation identifies the MIL as a dynamic section of NTPDases that is potentially involved in regulation of catalysis. | ||
| + | |||
| + | Crystal structure of NTPDase2 in complex with the sulfoanthraquinone inhibitor PSB-071.,Zebisch M, Baqi Y, Schafer P, Muller CE, Strater N J Struct Biol. 2014 Jan 21. pii: S1047-8477(14)00006-9. doi:, 10.1016/j.jsb.2014.01.005. PMID:24462745<ref>PMID:24462745</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4cd1" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Ectonucleoside triphosphate diphosphohydrolase|Ectonucleoside triphosphate diphosphohydrolase]] | *[[Ectonucleoside triphosphate diphosphohydrolase|Ectonucleoside triphosphate diphosphohydrolase]] | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Current revision
RnNTPDase2 in complex with PSB-071
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