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3nfy

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[[Image:3nfy.png|left|200px]]
 
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{{STRUCTURE_3nfy| PDB=3nfy | SCENE= }}
{{STRUCTURE_3nfy| PDB=3nfy | SCENE= }}
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===The Structure of Human Bisphosphoglycerate Mutase to 1.94A===
===The Structure of Human Bisphosphoglycerate Mutase to 1.94A===
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{{ABSTRACT_PUBMED_21045285}}
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{{ABSTRACT_PUBMED_21045285}}
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==Disease==
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[[http://www.uniprot.org/uniprot/PMGE_HUMAN PMGE_HUMAN]] Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:[http://omim.org/entry/222800 222800]]. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.<ref>PMID:2542247</ref><ref>PMID:1421379</ref><ref>PMID:15054810</ref>
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==Function==
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[[http://www.uniprot.org/uniprot/PMGE_HUMAN PMGE_HUMAN]] Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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<ref group="xtra">PMID:021045285</ref><references group="xtra"/>
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<ref group="xtra">PMID:021045285</ref><references group="xtra"/><references/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Nairn, J.]]
[[Category: Nairn, J.]]

Revision as of 05:35, 25 March 2013

Template:STRUCTURE 3nfy

Contents

The Structure of Human Bisphosphoglycerate Mutase to 1.94A

Template:ABSTRACT PUBMED 21045285

Disease

[PMGE_HUMAN] Defects in BPGM are the cause of bisphosphoglycerate mutase deficiency (BPGMD) [MIM:222800]. A disease characterized by hemolytic anemia, splenomegaly, cholelithiasis and cholecystitis.[1][2][3]

Function

[PMGE_HUMAN] Plays a major role in regulating hemoglobin oxygen affinity by controlling the levels of its allosteric effector 2,3-bisphosphoglycerate (2,3-BPG). Also exhibits mutase (EC 5.4.2.1) and phosphatase (EC 3.1.3.13) activities.

About this Structure

3nfy is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  • Patterson A, Price NC, Nairn J. Unliganded structure of human bisphosphoglycerate mutase reveals side-chain movements induced by ligand binding. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Nov 1;66(Pt, 11):1415-20. Epub 2010 Oct 27. PMID:21045285 doi:10.1107/S1744309110035475
  1. ↑ Rosa R, Blouquit Y, Calvin MC, Prome D, Prome JC, Rosa J. Isolation, characterization, and structure of a mutant 89 Arg----Cys bisphosphoglycerate mutase. Implication of the active site in the mutation. J Biol Chem. 1989 May 15;264(14):7837-43. PMID:2542247
  2. ↑ Lemarchandel V, Joulin V, Valentin C, Rosa R, Galacteros F, Rosa J, Cohen-Solal M. Compound heterozygosity in a complete erythrocyte bisphosphoglycerate mutase deficiency. Blood. 1992 Nov 15;80(10):2643-9. PMID:1421379
  3. ↑ Hoyer JD, Allen SL, Beutler E, Kubik K, West C, Fairbanks VF. Erythrocytosis due to bisphosphoglycerate mutase deficiency with concurrent glucose-6-phosphate dehydrogenase (G-6-PD) deficiency. Am J Hematol. 2004 Apr;75(4):205-8. PMID:15054810 doi:10.1002/ajh.20014

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