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Title 

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

Authors 

Hyo Jin KangSuk Kyeong JungSeung Jun KimSang Jeon Chung

Publisher 

International Union of Crystallography

Issue Date 

2008

Citation 

Acta Crystallographica. Section D, Biological Crystallography, vol. 64, no. 6, pp. 651-657

Keywords 

α-enolasesautoimmune diseasecancer metastasisinfectionplasminogen receptorscomplementary DNADNA binding proteinENO1 protein, humanenolaseplasmin

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.

Citation 

Acta Crystallographica. Section D, Biological Crystallography, 64(6): 651-657

ISSN 

0907-4449

Link 

http://dx.doi.org/10.1107/S0907444908008561

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2019-05-02


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