Structure-Function Relationships of C-Type Lectin-Related Proteins | Zendy

Takashi Morita | Zendy

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Structure-Function Relationships of C-Type Lectin-Related Proteins

Author(s) -

Takashi Morita

Publication year - 2005

Publication title -

pathophysiology of haemostasis and thrombosis

Language(s) - English

Resource type - Journals

eISSN - 1424-8840

pISSN - 1424-8832

DOI - 10.1159/000092415

Subject(s) - c type lectin , lectin , coagulation , chemistry , factor ix , function (biology) , glycoprotein , biochemistry , domain (mathematical analysis) , biology , microbiology and biotechnology , medicine , mathematical analysis , mathematics , psychiatry

The structural and functional studies of the first identified C-type lectin-like protein (CLP), blood coagulation factor IX/factor X-binding protein (IX/X-bp), have been instrumental in defining how new functionally heterodimeric CLPs are generated from monomeric carbohydrate recognition domain in C-type lectins by three-dimensional domain swapping. The crystal structures of gamma-carboxyglutamic acid domains of coagulation factors X and IX have recently been clarified in structural studies of complexes between the gamma-carboxyglutamic acid domain of factors X and X-bp (a venom CLP) and between the gamma-carboxyglutamic acid domain of factors IX and IX-bp (a venom CLP).

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