2ybe: Difference between revisions
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{{STRUCTURE_2ybe| PDB=2ybe | SCENE= }} | {{STRUCTURE_2ybe| PDB=2ybe | SCENE= }} | ||
===THE STRUCTURE OF THE FULLY CLOSED CONFORMATION OF HUMAN PGK IN COMPLEX WITH L-ADP, 3PG AND THE TSA ALUMINIUM TETRAFLUORIDE AT 2.0 A RESOLUTION=== | |||
{{ABSTRACT_PUBMED_21549713}} | |||
=== | ==Disease== | ||
[[http://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] Defects in PGK1 are the cause of phosphoglycerate kinase 1 deficiency (PGK1D) [MIM:[http://omim.org/entry/300653 300653]]. It is a condition with a highly variable clinical phenotype that includes hemolytic anemia, rhabdomyolysis, myopathy and neurologic involvement. Patients can express one or more of these manifestations.<ref>PMID:8673469</ref><ref>PMID:8043870</ref><ref>PMID:8615693</ref><ref>PMID:9744480</ref><ref>PMID:2001457</ref><ref>PMID:1586722</ref><ref>PMID:1547346</ref><ref>PMID:6941312</ref><ref>PMID:6933565</ref> | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/PGK1_HUMAN PGK1_HUMAN]] In addition to its role as a glycolytic enzyme, it seems that PGK-1 acts as a polymerase alpha cofactor protein (primer recognition protein). | |||
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID:021549713</ref><references group="xtra"/> | <ref group="xtra">PMID:021549713</ref><references group="xtra"/><references/> | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Phosphoglycerate kinase]] | [[Category: Phosphoglycerate kinase]] | ||
