A copy of this work was available on the public web and has been preserved in the Wayback Machine. The capture dates from 2018; you can also visit the original URL.
The file type is application/pdf
.
3-Dimensional Structure of Coagulation Factor Binding Protein Which Has C-type Lectin Domains
C型レクチンドメインをもつ血液凝固因子結合タンパク質の立体構造
1998
Seibutsu Butsuri
C型レクチンドメインをもつ血液凝固因子結合タンパク質の立体構造
Blood coagulation factors IX/X-binding protein (IX/X-bp) is a heterodimer consisting of two homologous subunits. The amino acid sequence of each subunit is homologous to the carbohydrate-recognition domain of C-type lectin (C-type CRD), although IX/X-bp has no lectin activity. Crystal structure of IX/X-bp shows that a central loop projects into the adjoining subunit and contributes to an intertwinned dimer in a manner similar to 3D domain swapping. The exchange of the loop complete the C-type
doi:10.2142/biophys.38.240
fatcat:m52goadhqrfmzoyf2gaiijnc7e