Structure-function relationships of C-type lectin-related proteins.
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).
Morita
Takashi
T
Department of Biochemistry, Meiji Pharmaceutical University, Noshio, Kiyose, Tokyo, Japan. tmorita@my-pharm.ac.jp
D015055:1-Carboxyglutamic Acid / Q000737:chemistry; D000818:Animals; D003435:Crotalid Venoms / Q000737:chemistry; D005164:Factor IX / Q000737:chemistry; D005170:Factor X / Q000737:chemistry; D006801:Humans; D037181:Lectins, C-Type / Q000737:chemistry*; D030162:Reptilian Proteins / Q000737:chemistry; D013329:Structure-Activity Relationship
D003435:Crotalid Venoms; D037181:Lectins, C-Type; D030162:Reptilian Proteins; C099136:factor IX-factor X-binding protein, Echis carinatus; C070302:factor IX-factor X-binding protein, Crotalinae; D015055:1-Carboxyglutamic Acid; D005164:Factor IX; D005170:Factor X