2vgf

From Proteopedia

proteopedia linkproteopedia link

Template:STRUCTURE 2vgf

Contents 1 HUMAN ERYTHROCYTE PYRUVATE KINASE: T384M MUTANT 2 Disease 3 Function 4 About this Structure 5 See Also 6 Reference

HUMAN ERYTHROCYTE PYRUVATE KINASE: T384M MUTANT

Template:ABSTRACT PUBMED 11960989

Disease

[KPYR_HUMAN] Defects in PKLR are the cause of pyruvate kinase hyperactivity (PKHYP) [MIM:102900]; also known as high red cell ATP syndrome. This autosomal dominant phenotype is characterized by increase of red blood cell ATP.^[1] Defects in PKLR are the cause of pyruvate kinase deficiency of red cells (PKRD) [MIM:266200]. A frequent cause of hereditary non-spherocytic hemolytic anemia. Clinically, pyruvate kinase-deficient patients suffer from a highly variable degree of chronic hemolysis, ranging from severe neonatal jaundice and fatal anemia at birth, severe transfusion-dependent chronic hemolysis, moderate hemolysis with exacerbation during infection, to a fully compensated hemolysis without apparent anemia.

Function

[KPYR_HUMAN] Plays a key role in glycolysis (By similarity).

About this Structure

2vgf is a 4 chain structure with sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1liw. Full crystallographic information is available from OCA.

See Also

• Pyruvate Kinase

Reference

• Valentini G, Chiarelli LR, Fortin R, Dolzan M, Galizzi A, Abraham DJ, Wang C, Bianchi P, Zanella A, Mattevi A. Structure and function of human erythrocyte pyruvate kinase. Molecular basis of nonspherocytic hemolytic anemia. J Biol Chem. 2002 Jun 28;277(26):23807-14. Epub 2002 Apr 17. PMID:11960989 doi:10.1074/jbc.M202107200

1. ↑ Beutler E, Westwood B, van Zwieten R, Roos D. G-->T transition at cDNA nt 110 (K37Q) in the PKLR (pyruvate kinase) gene is the molecular basis of a case of hereditary increase of red blood cell ATP. Hum Mutat. 1997;9(3):282-5. PMID:9090535 doi:<282::AID-HUMU13>3.0.CO;2-Z 10.1002/(SICI)1098-1004(1997)9:3<282::AID-HUMU13>3.0.CO;2-Z