Title : Crystallization of the N-terminal domain of human sex hormone-binding globulin, the major sex steroid carrier in blood.

Pub. Date : 1999 Dec

PMID : 10666590






4 Functional Relationships(s)
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Protein Name
Organism
1 The amino-teminal laminin G-like domain of human sex hormone-binding globulin (SHBG), which contains the steroid-binding site and the dimerization domain, has been produced in Escherichia coli, purified to homogeneity and crystallized in complex with 5alpha--dihydrotestosterone (DHT) in two different crystal forms. Dihydrotestosterone sex hormone binding globulin Homo sapiens
2 The amino-teminal laminin G-like domain of human sex hormone-binding globulin (SHBG), which contains the steroid-binding site and the dimerization domain, has been produced in Escherichia coli, purified to homogeneity and crystallized in complex with 5alpha--dihydrotestosterone (DHT) in two different crystal forms. Dihydrotestosterone sex hormone binding globulin Homo sapiens
3 The amino-teminal laminin G-like domain of human sex hormone-binding globulin (SHBG), which contains the steroid-binding site and the dimerization domain, has been produced in Escherichia coli, purified to homogeneity and crystallized in complex with 5alpha--dihydrotestosterone (DHT) in two different crystal forms. Dihydrotestosterone sex hormone binding globulin Homo sapiens
4 The amino-teminal laminin G-like domain of human sex hormone-binding globulin (SHBG), which contains the steroid-binding site and the dimerization domain, has been produced in Escherichia coli, purified to homogeneity and crystallized in complex with 5alpha--dihydrotestosterone (DHT) in two different crystal forms. Dihydrotestosterone sex hormone binding globulin Homo sapiens