1d2s

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(New page: 200px<br /> <applet load="1d2s" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d2s, resolution 1.55&Aring;" /> '''CRYSTAL STRUCTURE O...)
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[[Image:1d2s.gif|left|200px]]<br /><applet load="1d2s" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1d2s" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1d2s, resolution 1.55&Aring;" />
caption="1d2s, resolution 1.55&Aring;" />
'''CRYSTAL STRUCTURE OF THE N-TERMINAL LAMININ G-LIKE DOMAIN OF SHBG IN COMPLEX WITH DIHYDROTESTOSTERONE'''<br />
'''CRYSTAL STRUCTURE OF THE N-TERMINAL LAMININ G-LIKE DOMAIN OF SHBG IN COMPLEX WITH DIHYDROTESTOSTERONE'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1D2S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and DHT as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1D2S with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb92_1.html Anabolic Steroids]]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1D2S OCA].
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1D2S is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=DHT:'>DHT</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. The following page contains interesting information on the relation of 1D2S with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb92_1.html Anabolic Steroids]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D2S OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Avvakumov, G.V.]]
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[[Category: Avvakumov, G V.]]
[[Category: Dales, D.]]
[[Category: Dales, D.]]
[[Category: Grishkovskaya, I.]]
[[Category: Grishkovskaya, I.]]
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[[Category: Hammond, G.L.]]
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[[Category: Hammond, G L.]]
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[[Category: Muller, Y.A.]]
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[[Category: Muller, Y A.]]
[[Category: Sklenar, G.]]
[[Category: Sklenar, G.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: steroid transport]]
[[Category: steroid transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:27:58 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:12:21 2008''

Revision as of 10:12, 21 February 2008


1d2s, resolution 1.55Å

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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 and 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

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