Structure of human α-enolase (hENO1), a multifunctional glycolytic enzyme

Cited 80 time in scopus
Metadata Downloads
Title
Structure of human α-enolase (hENO1), a multifunctional glycolytic enzyme
Author(s)
Hyo Jin Kang; Suk Kyeong Jung; Seung Jun Kim; Sang Jeon Chung
Bibliographic Citation
Acta Crystallographica Section D-Biological Crystallography, vol. 64, no. 6, pp. 651-657
Publication Year
2008
Abstract
Aside from its enzymatic function in the glycolytic pathway, α-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 ? 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.
Keyword
α-enolasesautoimmune diseasecancer metastasisinfectionplasminogen receptors
ISSN
0907-4449
Publisher
Int Union Crystallography
DOI
http://dx.doi.org/10.1107/S0907444908008561
Type
Article
Appears in Collections:
Critical Diseases Diagnostics Convergence Research Center > 1. Journal Articles
Files in This Item:
  • There are no files associated with this item.


Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.