Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme. Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] Journal article | | Title | Structure of human alpha-enolase (hENO1), a multifunctional glycolytic enzyme. | | Author(s) | Kang HJ, Jung SK, Kim SJ, Chung SJ | | Institution | BioNanotechnology Research Center, Korea Research Institute of Bioscience and Biotechnology and Division of Nanobiotechnology, Korea University of Science and Technology (UST), Yuseong, Daejeon 305-333, Republic of Korea. | | Source | Acta Crystallogr D Biol Crystallogr 2008 Jun; 64(Pt 6):651-7. | | 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. | | Language | eng | | Pub Type(s) | Journal Article
| | PubMed ID | 18560153 |
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