1d2s

<table><tr><td colspan='2'>[[1d2s]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. The August 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Anabolic Steroids'' by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_8 10.2210/rcsb_pdb/mom_2007_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D2S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1D2S FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHT:5-ALPHA-DIHYDROTESTOSTERONE'>DHT</scene></td></tr>

[[https://www.uniprot.org/uniprot/SHBG_HUMAN SHBG_HUMAN]] Functions as an androgen transport protein, but may also be involved in receptor mediated processes. Each dimer binds one molecule of steroid. Specific for 5-alpha-dihydrotestosterone, testosterone, and 17-beta-estradiol. Regulates the plasma metabolic clearance rate of steroid hormones by controlling their plasma concentration.

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== Publication Abstract from PubMed ==

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.

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<ref>PMID:10675319</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

<references/>

[[Category: Human]]

[[Category: Avvakumov, G V]]

[[Category: Dales, D]]

[[Category: Grishkovskaya, I]]

[[Category: Hammond, G L]]

[[Category: Muller, Y A]]

[[Category: Sklenar, G]]

[[Category: Transport protein]]