1d2s
From Proteopedia
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CRYSTAL STRUCTURE OF THE N-TERMINAL LAMININ G-LIKE DOMAIN OF SHBG IN COMPLEX WITH DIHYDROTESTOSTERONE
Overview
Human sex hormone-binding globulin (SHBG) transports sex steroids in blood, and regulates their access to target tissues. In biological fluids, SHBG, exists as a homodimer and each monomer comprises two laminin G-like, domains (G domains). The crystal structure of the N-terminal G domain of, SHBG in complex with 5alpha-dihydrotestosterone at 1.55 A resolution, reveals both the architecture of the steroid-binding site and the, quaternary structure of the dimer. We also show that G domains have, jellyroll topology and are structurally related to pentraxin. In each SHBG, monomer, the steroid intercalates into a hydrophobic pocket within the, beta-sheet sandwich. The steroid and a 20 A distant calcium ion are not, located at the dimer interface. Instead, two separate steroid-binding, pockets and calcium-binding sites exist per dimer. The structure displays, intriguing disorder for loop segment Pro130-Arg135. In all other jellyroll, proteins, this loop is well ordered. If modelled accordingly, it covers, the steroid-binding site and could thereby regulate access of ligands to, the binding pocket.
About this Structure
1D2S is a Single protein structure of sequence from Homo sapiens with CA and DHT as ligands. The following page contains interesting information on the relation of 1D2S with [Anabolic Steroids]. Full crystallographic information is available from OCA.
Reference
Crystal structure of human sex hormone-binding globulin: steroid transport by a laminin G-like domain., Grishkovskaya I, Avvakumov GV, Sklenar G, Dales D, Hammond GL, Muller YA, EMBO J. 2000 Feb 15;19(4):504-12. PMID:10675319
Page seeded by OCA on Mon Nov 12 16:27:58 2007
