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Title 

Homology modeling of the receptor binding domain of human thrombopoietin

Authors 

Jin Soo SongHeung Rok ParkHyo Jeong HongMyeong Hee YuSeong Eon Ryu

Publisher 

Springer Verlag (Germany)

Issue Date 

1998

Citation 

Journal of Computer Aided Molecular Design, vol. 12, no. 0, pp. 419-424

Keywords 

comparative modelingcytokinefour-helix bundleplateletreceptor-ligand interaction

Abstract 

Platelet production in blood is regulated by a lineage specific humoral factor, thrombopoietin (TPO). The amino terminal domain of TPO (TPO-N) is responsible for the signal transduction mediated by the TPO receptor, c-mpl. From the predicted length of helices we found that TPO-N belongs to the long-chain subfamily of the four-helix bundle cytokine family. We built a three dimensional model of TPO-N by a comparative homology modeling procedure. The four helices of TPO-N with an up-up-down-down topology are stabilized by a tightly packed central hydrophobic core and the extended loop AB makes an additional hydrophobic core with helices B and D outside of the four helix bundle scaffold. An interpretation of the previous site directed mutageneses results in light of the model enabled us to identify two isolated receptor binding sites. The surface made of Lys 136, Lys 138 and Lys 140 in helix D, and Pro 42 and Glu 50 in loop AB forms the first receptor binding site, while the surface of Asp 8, Arg 10 and Lys14 in helix A represents the second binding site for the sequential receptor oligomerization.

ISSN 

0920-654X

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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