1xwd
From Proteopedia
(New page: 200px<br /> <applet load="1xwd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xwd, resolution 2.92Å" /> '''Crystal Structure o...) |
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| - | [[Image:1xwd.gif|left|200px]]<br /> | + | [[Image:1xwd.gif|left|200px]]<br /><applet load="1xwd" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xwd" size=" | + | |
caption="1xwd, resolution 2.92Å" /> | caption="1xwd, resolution 2.92Å" /> | ||
'''Crystal Structure of Human Follicle Stimulating Hormone Complexed with its Receptor'''<br /> | '''Crystal Structure of Human Follicle Stimulating Hormone Complexed with its Receptor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Follicle-stimulating hormone (FSH) is central to reproduction in mammals. | + | Follicle-stimulating hormone (FSH) is central to reproduction in mammals. It acts through a G-protein-coupled receptor on the surface of target cells to stimulate testicular and ovarian functions. We present here the 2.9-A-resolution structure of a partially deglycosylated complex of human FSH bound to the extracellular hormone-binding domain of its receptor (FSHR(HB)). The hormone is bound in a hand-clasp fashion to an elongated, curved receptor. The buried interface of the complex is large (2,600 A2) and has a high charge density. Our analysis suggests that all glycoprotein hormones bind to their receptors in this mode and that binding specificity is mediated by key interaction sites involving both the common alpha- and hormone-specific beta-subunits. On binding, FSH undergoes a concerted conformational change that affects protruding loops implicated in receptor activation. The FSH-FSHR(HB) complexes form dimers in the crystal and at high concentrations in solution. Such dimers may participate in transmembrane signal transduction. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XWD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1XWD is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1XWD OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Fan, Q | + | [[Category: Fan, Q R.]] |
| - | [[Category: Hendrickson, W | + | [[Category: Hendrickson, W A.]] |
[[Category: NAG]] | [[Category: NAG]] | ||
[[Category: SO4]] | [[Category: SO4]] | ||
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[[Category: leucine-rich repeats]] | [[Category: leucine-rich repeats]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:59:21 2008'' |
Revision as of 13:59, 21 February 2008
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Crystal Structure of Human Follicle Stimulating Hormone Complexed with its Receptor
Contents |
Overview
Follicle-stimulating hormone (FSH) is central to reproduction in mammals. It acts through a G-protein-coupled receptor on the surface of target cells to stimulate testicular and ovarian functions. We present here the 2.9-A-resolution structure of a partially deglycosylated complex of human FSH bound to the extracellular hormone-binding domain of its receptor (FSHR(HB)). The hormone is bound in a hand-clasp fashion to an elongated, curved receptor. The buried interface of the complex is large (2,600 A2) and has a high charge density. Our analysis suggests that all glycoprotein hormones bind to their receptors in this mode and that binding specificity is mediated by key interaction sites involving both the common alpha- and hormone-specific beta-subunits. On binding, FSH undergoes a concerted conformational change that affects protruding loops implicated in receptor activation. The FSH-FSHR(HB) complexes form dimers in the crystal and at high concentrations in solution. Such dimers may participate in transmembrane signal transduction.
Disease
Known diseases associated with this structure: Follicle-stimulating hormone deficiency, isolated OMIM:[136530], Ovarian dysgenesis 1 OMIM:[136435], Ovarian hyperstimulation syndrome OMIM:[136435], Ovarian response to FSH stimulation OMIM:[136435], Ovarian sex cord tumors OMIM:[136435]
About this Structure
1XWD is a Protein complex structure of sequences from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Structure of human follicle-stimulating hormone in complex with its receptor., Fan QR, Hendrickson WA, Nature. 2005 Jan 20;433(7023):269-77. PMID:15662415
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