Abstract
Aside from its enzymatic function in the glycolytic pathway, alpha-enolase (ENO1) has been implicated in numerous diseases, including metastatic cancer, autoimmune disorders, ischaemia and bacterial infection. The disease-related roles of ENO1 are mostly attributed to its immunogenic capacity, DNA-binding ability and plasmin(ogen) receptor function, which are significantly affected by its three-dimensional structure and surface properties, rather than its enzymatic activity. Here, the crystal structure of human ENO1 (hENO1) is presented at 2.2 A resolution. Despite its high sequence similarity to other enolases, the hENO1 structure exhibits distinct surface properties, explaining its various activities, including plasmin(ogen) and DNA binding.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Base Sequence
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Biomarkers, Tumor / chemistry*
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Biomarkers, Tumor / genetics
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Biomarkers, Tumor / metabolism
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Catalytic Domain
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Crystallography, X-Ray
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DNA Primers / genetics
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DNA, Complementary / genetics
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DNA, Complementary / metabolism
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DNA-Binding Proteins / chemistry*
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DNA-Binding Proteins / genetics
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DNA-Binding Proteins / metabolism
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Fibrinolysin / metabolism
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Humans
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Models, Molecular
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Phosphopyruvate Hydratase / chemistry*
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Phosphopyruvate Hydratase / genetics
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Phosphopyruvate Hydratase / metabolism
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Plasminogen / metabolism
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Protein Structure, Secondary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Static Electricity
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Tumor Suppressor Proteins / chemistry*
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Tumor Suppressor Proteins / genetics
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Tumor Suppressor Proteins / metabolism
Substances
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Biomarkers, Tumor
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DNA Primers
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DNA, Complementary
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DNA-Binding Proteins
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Recombinant Proteins
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Tumor Suppressor Proteins
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Plasminogen
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Fibrinolysin
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ENO1 protein, human
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Phosphopyruvate Hydratase