1f5f
From Proteopedia
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|PDB= 1f5f |SIZE=350|CAPTION= <scene name='initialview01'>1f5f</scene>, resolution 1.7Å | |PDB= 1f5f |SIZE=350|CAPTION= <scene name='initialview01'>1f5f</scene>, resolution 1.7Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DHT:DIHYDROTESTOSTERONE'>DHT</scene>, <scene name='pdbligand=IPA:ISOPROPYL+ALCOHOL'>IPA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1d2s|1d2s]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1f5f FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f5f OCA], [http://www.ebi.ac.uk/pdbsum/1f5f PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1f5f RCSB]</span> | ||
}} | }} | ||
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[[Category: Hammond, G L.]] | [[Category: Hammond, G L.]] | ||
[[Category: Muller, Y A.]] | [[Category: Muller, Y A.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: DHT]] | ||
| - | [[Category: IPA]] | ||
| - | [[Category: ZN]] | ||
[[Category: jellyroll]] | [[Category: jellyroll]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:16:16 2008'' |
Revision as of 17:16, 30 March 2008
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| , resolution 1.7Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1d2s
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE N-TERMINAL G-DOMAIN OF SHBG IN COMPLEX WITH ZINC
Overview
One calcium-binding site (site I) and a second poorly defined metal-binding site (site II) have been observed previously within the amino-terminal laminin G-like domain (G domain) of human sex hormone-binding globulin (SHBG). By soaking crystals of this structure in 2.5 mm ZnCl(2), site II and a new metal-binding site (site III) were found to bind Zn(2+). Site II is located close to the steroid-binding site, and Zn(2+) is coordinated by the side chains of His(83) and His(136) and the carboxylate group of Asp(65). In this site, Zn(2+) prevents Asp(65) from interacting with the steroid 17beta-hydroxy group and alters the conformations of His(83) and His(136), as well as a disordered region over the steroid-binding site. Site III is formed by the side chains of His(101) and the carboxylate group of Asp(117), and the distance between them (2.7 A) is increased to 3.7 A in the presence of Zn(2+). The affinity of SHBG for estradiol is reduced in the presence of 0. 1-1 mm Zn(2+), whereas its affinity for androgens is unchanged, and chemically-related metal ions (Cd(2+) and Hg(2+)) have similar but less pronounced effects. This is not observed when Zn(2+) coordination at site II is modified by substituting Gln for His(136). An alteration in the steroid-binding specificity of human SHBG by Zn(2+) occupancy of site II may be relevant in male reproductive tissues where zinc concentrations are very high.
About this Structure
1F5F is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Steroid-binding specificity of human sex hormone-binding globulin is influenced by occupancy of a zinc-binding site., Avvakumov GV, Muller YA, Hammond GL, J Biol Chem. 2000 Aug 25;275(34):25920-5. PMID:10859323
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