1lho

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[[Image:1lho.gif|left|200px]]<br /><applet load="1lho" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1lho.gif|left|200px]]
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caption="1lho, resolution 2.00&Aring;" />
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'''CRYSTAL STRUCTURE OF THE N-TERMINAL LG-DOMAIN OF SHBG IN COMPLEX WITH 5ALPHA-ANDROSTANE-3BETA,17BETA-DIOL'''<br />
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{{Structure
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|PDB= 1lho |SIZE=350|CAPTION= <scene name='initialview01'>1lho</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=AOM:5-ALPHA-ANDROSTANE-3-BETA,17BETA-DIOL'>AOM</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF THE N-TERMINAL LG-DOMAIN OF SHBG IN COMPLEX WITH 5ALPHA-ANDROSTANE-3BETA,17BETA-DIOL'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1LHO 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=AOM:'>AOM</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LHO OCA].
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1LHO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LHO OCA].
==Reference==
==Reference==
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Steroid ligands bind human sex hormone-binding globulin in specific orientations and produce distinct changes in protein conformation., Grishkovskaya I, Avvakumov GV, Hammond GL, Catalano MG, Muller YA, J Biol Chem. 2002 Aug 30;277(35):32086-93. Epub 2002 Jun 13. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12065592 12065592]
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Steroid ligands bind human sex hormone-binding globulin in specific orientations and produce distinct changes in protein conformation., Grishkovskaya I, Avvakumov GV, Hammond GL, Catalano MG, Muller YA, J Biol Chem. 2002 Aug 30;277(35):32086-93. Epub 2002 Jun 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12065592 12065592]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: shbg]]
[[Category: shbg]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:45:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:31:02 2008''

Revision as of 10:31, 20 March 2008

Image:1lho.gif


PDB ID 1lho

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE N-TERMINAL LG-DOMAIN OF SHBG IN COMPLEX WITH 5ALPHA-ANDROSTANE-3BETA,17BETA-DIOL


Overview

The amino-terminal laminin G-like domain of human sex hormone-binding globulin (SHBG) contains a single high affinity steroid-binding site. Crystal structures of this domain in complex with several different steroid ligands have revealed that estradiol occupies the SHBG steroid-binding site in an opposite orientation when compared with 5 alpha-dihydrotestosterone or C19 androgen metabolites (5 alpha-androstan-3 beta,17 beta-diol and 5 alpha-androstan-3 beta,17 alpha-diol) or the synthetic progestin levonorgestrel. Substitution of specific residues within the SHBG steroid-binding site confirmed that Ser(42) plays a key role in determining high affinity interactions by hydrogen bonding to functional groups at C3 of the androstanediols and levonorgestrel and the hydroxyl at C17 of estradiol. Among residues participating in the hydrogen bond network with hydroxy groups at C17 of C19 steroids or C3 of estradiol, Asp(65) appears to be the most important. The different binding mode of estradiol is associated with a difference in the position/orientation of residues (Leu(131) and Lys(134)) in the loop segment (Leu(131)-His(136)) that covers the steroid-binding site as well as others (Leu(171)-Lys(173) and Trp(84)) on the surface of human SHBG and may provide a basis for ligand-dependent interactions between SHBG and other macromolecules. These new crystal structures have also enabled us to construct a simple space-filling model that can be used to predict the characteristics of novel SHBG ligands.

About this Structure

1LHO is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Steroid ligands bind human sex hormone-binding globulin in specific orientations and produce distinct changes in protein conformation., Grishkovskaya I, Avvakumov GV, Hammond GL, Catalano MG, Muller YA, J Biol Chem. 2002 Aug 30;277(35):32086-93. Epub 2002 Jun 13. PMID:12065592

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