3ffs

From Proteopedia

(Difference between revisions)

Revision as of 09:06, 25 December 2014

The Crystal Structure of Cryptosporidium parvum Inosine-5'-Monophosphate Dehydrogenase

Structural highlights

3ffs is a 4 chain structure with sequence from Cryptosporidium parvum. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	IMPDH, 56k.02 (Cryptosporidium parvum)
Activity:	IMP dehydrogenase, with EC number 1.1.1.205
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[Q8T6T2_CRYPV] 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.[HAMAP-Rule:MF_03156]^[1]

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

Cryptosporidium parvum is a potential biowarfare agent, an important AIDS pathogen, and a major cause of diarrhea and malnutrition. No vaccines or effective drug treatment exist to combat Cryptosporidium infection. This parasite relies on inosine 5'-monophosphate dehydrogenase (IMPDH) to obtain guanine nucleotides, and inhibition of this enzyme blocks parasite proliferation. Here, we report the first crystal structures of CpIMPDH. These structures reveal the structural basis of inhibitor selectivity and suggest a strategy for further optimization. Using this information, we have synthesized low-nanomolar inhibitors that display 10(3) selectivity for the parasite enzyme over human IMPDH2.

The Structural Basis of Cryptosporidium -Specific IMP Dehydrogenase Inhibitor Selectivity.,Macpherson IS, Kirubakaran S, Gorla SK, Riera TV, D'Aquino JA, Zhang M, Cuny GD, Hedstrom L J Am Chem Soc. 2010 Jan 6. PMID:20052976^[2]

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

References

↑ Umejiego NN, Li C, Riera T, Hedstrom L, Striepen B. Cryptosporidium parvum IMP dehydrogenase: identification of functional, structural, and dynamic properties that can be exploited for drug design. J Biol Chem. 2004 Sep 24;279(39):40320-7. Epub 2004 Jul 21. PMID:15269207 doi:10.1074/jbc.M407121200
↑ Macpherson IS, Kirubakaran S, Gorla SK, Riera TV, D'Aquino JA, Zhang M, Cuny GD, Hedstrom L. The Structural Basis of Cryptosporidium -Specific IMP Dehydrogenase Inhibitor Selectivity. J Am Chem Soc. 2010 Jan 6. PMID:20052976 doi:10.1021/ja909947a

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/3ffs"

@@ Line 7: / Line 7: @@
 <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=3ffs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ffs OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ffs RCSB], [http://www.ebi.ac.uk/pdbsum/3ffs PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/Q8T6T2_CRYPV Q8T6T2_CRYPV]] 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.[HAMAP-Rule:MF_03156]<ref>PMID:15269207</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

3ffs

From Proteopedia

Revision as of 09:06, 25 December 2014

The Crystal Structure of Cryptosporidium parvum Inosine-5'-Monophosphate Dehydrogenase

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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