1jr1

From Proteopedia

(Difference between revisions)

Revision as of 09:45, 4 October 2017

Crystal structure of Inosine Monophosphate Dehydrogenase in complex with Mycophenolic Acid

Structural highlights

1jr1 is a 2 chain structure with sequence from Cho cell lines. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Related:	1ak5, 1b3o, 1zfj
Activity:	IMP dehydrogenase, with EC number 1.1.1.205
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[IMDH2_CRIGR] Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism (By similarity). It may also have a role in the development of malignancy and the growth progression of some tumors.[HAMAP-Rule:MF_03156]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The structure of inosine-5'-monophosphate dehydrogenase (IMPDH) in complex with IMP and mycophenolic acid (MPA) has been determined by X-ray diffraction. IMPDH plays a central role in B and T lymphocyte replication. MPA is a potent IMPDH inhibitor and the active metabolite of an immunosuppressive drug recently approved for the treatment of allograft rejection. IMPDH comprises two domains: a core domain, which is an alpha/beta barrel and contains the active site, and a flanking domain. The complex, in combination with mutagenesis and kinetic data, provides a structural basis for understanding the mechanism of IMPDH activity and indicates that MPA inhibits IMPDH by acting as a replacement for the nicotinamide portion of the nicotinamide adenine dinucleotide cofactor and a catalytic water molecule.

Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid.,Sintchak MD, Fleming MA, Futer O, Raybuck SA, Chambers SP, Caron PR, Murcko MA, Wilson KP Cell. 1996 Jun 14;85(6):921-30. PMID:8681386^[1]

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

References

↑ Sintchak MD, Fleming MA, Futer O, Raybuck SA, Chambers SP, Caron PR, Murcko MA, Wilson KP. Structure and mechanism of inosine monophosphate dehydrogenase in complex with the immunosuppressant mycophenolic acid. Cell. 1996 Jun 14;85(6):921-30. PMID:8681386

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1jr1"

@@ Line 1: / Line 1: @@
 ==Crystal structure of Inosine Monophosphate Dehydrogenase in complex with Mycophenolic Acid==
 <StructureSection load='1jr1' size='340' side='right' caption='[[1jr1]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ak5|1ak5]], [[1b3o|1b3o]], [[1zfj|1zfj]]</td></tr>
 <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/IMP_dehydrogenase IMP dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.1.205 1.1.1.205] </span></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=1jr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jr1 OCA], [http://pdbe.org/1jr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jr1 RCSB], [http://www.ebi.ac.uk/pdbsum/1jr1 PDBsum]</span></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=1jr1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jr1 OCA], [http://pdbe.org/1jr1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jr1 RCSB], [http://www.ebi.ac.uk/pdbsum/1jr1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jr1 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 18: / Line 19: @@
     <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/chain_selection.php?pdb_ID=2ata ConSurf].
+</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=1jr1 ConSurf].
 <div style="clear:both"></div>
 <div style="background-color:#fffaf0;">

1jr1

From Proteopedia

Revision as of 09:45, 4 October 2017

Crystal structure of Inosine Monophosphate Dehydrogenase in complex with Mycophenolic Acid

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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