Crystal structure of streptokinase β‐domain | Zendy

Wang Xiaoqiang | Zendy; Tang Jordan | Zendy; Hunter Bret | Zendy; Zhang Xuejun C. | Zendy

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Crystal structure of streptokinase β‐domain

Author(s) -

Wang Xiaoqiang,

Tang Jordan,

Hunter Bret,

Zhang Xuejun C.

Publication year - 1999

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/s0014-5793(99)01214-4

Subject(s) - streptokinase , dimer , activator (genetics) , chemistry , crystal structure , domain (mathematical analysis) , protein structure , recombinant dna , kringle domain , plasminogen activator , biophysics , crystallography , stereochemistry , biochemistry , biology , gene , genetics , mathematical analysis , mathematics , organic chemistry , psychiatry , myocardial infarction , psychology

Streptokinase, a 47 kDa secreted protein of hemolytic strains of streptococci, is a human plasminogen activator and contains three structural domains linked by flexible loops. We describe here the crystal structure of the isolated streptokinase middle (SKβ) domain determined at 2.4 Å resolution. Among the functionally important structural features is a putative binding site for a kringle domain of plasminogen located at the tip of a fully exposed hairpin loop. The distribution of genetically conserved residues of SKβ is strongly correlated with their functions. The extensive interface of the SKβ dimer suggests that such dimers may also exist in solution for free SKβ.

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