3nfy: Difference between revisions
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{{STRUCTURE_3nfy| PDB=3nfy | SCENE= }} | {{STRUCTURE_3nfy| PDB=3nfy | SCENE= }} | ||
===The Structure of Human Bisphosphoglycerate Mutase to 1.94A=== | |||
{{ABSTRACT_PUBMED_21045285}} | |||
=== | ==Disease== | ||
[[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> | |||
==Function== | |||
[[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== | ||
| Line 14: | Line 16: | ||
==Reference== | ==Reference== | ||
<ref group="xtra">PMID:021045285</ref><references group="xtra"/> | <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
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
- ↑ 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
- ↑ 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
- ↑ 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
