1jdn
From Proteopedia
(New page: 200px<br /> <applet load="1jdn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jdn, resolution 2.9Å" /> '''Crystal Structure of...) |
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| - | [[Image:1jdn.gif|left|200px]]<br /> | + | [[Image:1jdn.gif|left|200px]]<br /><applet load="1jdn" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1jdn" size=" | + | |
caption="1jdn, resolution 2.9Å" /> | caption="1jdn, resolution 2.9Å" /> | ||
'''Crystal Structure of Hormone Receptor'''<br /> | '''Crystal Structure of Hormone Receptor'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Natriuretic peptides (NPs) are vasoactive cyclic-peptide hormones | + | Natriuretic peptides (NPs) are vasoactive cyclic-peptide hormones important in blood pressure regulation through interaction with natriuretic cell-surface receptors. We report the hormone-binding thermodynamics and crystal structures at 2.9 and 2.0 angstroms, respectively, of the extracellular domain of the unliganded human NP receptor (NPR-C) and its complex with CNP, a 22-amino acid NP. A single CNP molecule is bound in the interface of an NPR-C dimer, resulting in asymmetric interactions between the hormone and the symmetrically related receptors. Hormone binding induces a 20 angstrom closure between the membrane-proximal domains of the dimer. In each monomer, the opening of an interdomain cleft, which is tethered together by a linker peptide acting as a molecular spring, is likely a conserved allosteric trigger for intracellular signaling by the natriuretic receptor family. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1JDN 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 CL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JDN 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=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Chow, D | + | [[Category: Chow, D C.]] |
| - | [[Category: Garcia, K | + | [[Category: Garcia, K C.]] |
| - | [[Category: He, X | + | [[Category: He, X L.]] |
| - | [[Category: Martick, M | + | [[Category: Martick, M M.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: allosteric activation]] | [[Category: allosteric activation]] | ||
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[[Category: natriuretic peptide receptor]] | [[Category: natriuretic peptide receptor]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:26 2008'' |
Revision as of 11:21, 21 February 2008
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Crystal Structure of Hormone Receptor
Contents |
Overview
Natriuretic peptides (NPs) are vasoactive cyclic-peptide hormones important in blood pressure regulation through interaction with natriuretic cell-surface receptors. We report the hormone-binding thermodynamics and crystal structures at 2.9 and 2.0 angstroms, respectively, of the extracellular domain of the unliganded human NP receptor (NPR-C) and its complex with CNP, a 22-amino acid NP. A single CNP molecule is bound in the interface of an NPR-C dimer, resulting in asymmetric interactions between the hormone and the symmetrically related receptors. Hormone binding induces a 20 angstrom closure between the membrane-proximal domains of the dimer. In each monomer, the opening of an interdomain cleft, which is tethered together by a linker peptide acting as a molecular spring, is likely a conserved allosteric trigger for intracellular signaling by the natriuretic receptor family.
Disease
Known diseases associated with this structure: Hypertension, salt-resistant (1) OMIM:[108962]
About this Structure
1JDN is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Allosteric activation of a spring-loaded natriuretic peptide receptor dimer by hormone., He Xl, Chow Dc, Martick MM, Garcia KC, Science. 2001 Aug 31;293(5535):1657-62. PMID:11533490
Page seeded by OCA on Thu Feb 21 13:21:26 2008
