2h4z: Difference between revisions
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{{STRUCTURE_2h4z| PDB=2h4z | SCENE= }} | {{STRUCTURE_2h4z| PDB=2h4z | SCENE= }} | ||
===Human bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerate=== | |||
{{ABSTRACT_PUBMED_17052986}} | |||
=== | ==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:017052986</ref><references group="xtra"/> | <ref group="xtra">PMID:017052986</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Gong, W.]] | [[Category: Gong, W.]] | ||
Revision as of 20:56, 24 March 2013
Human bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerateHuman bisphosphoglycerate mutase complexed with 2,3-bisphosphoglycerate
Template:ABSTRACT PUBMED 17052986
DiseaseDisease
[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]
FunctionFunction
[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 StructureAbout this Structure
2h4z is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
See AlsoSee Also
ReferenceReference
- ↑ Wang Y, Liu L, Wei Z, Cheng Z, Lin Y, Gong W. Seeing the process of histidine phosphorylation in human bisphosphoglycerate mutase. J Biol Chem. 2006 Dec 22;281(51):39642-8. Epub 2006 Oct 18. PMID:17052986 doi:http://dx.doi.org/10.1074/jbc.M606421200
- ↑ 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