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1jdp

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[[Image:1jdp.gif|left|200px]]
[[Image:1jdp.gif|left|200px]]
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{{Structure
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|PDB= 1jdp |SIZE=350|CAPTION= <scene name='initialview01'>1jdp</scene>, resolution 2.0&Aring;
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The line below this paragraph, containing "STRUCTURE_1jdp", creates the "Structure Box" on the page.
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|LIGAND= <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>
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{{STRUCTURE_1jdp| PDB=1jdp | SCENE= }}
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|RELATEDENTRY=[[1jdn|1JDN]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1jdp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jdp OCA], [http://www.ebi.ac.uk/pdbsum/1jdp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1jdp RCSB]</span>
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'''Crystal Structure of Hormone/Receptor Complex'''
'''Crystal Structure of Hormone/Receptor Complex'''
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[[Category: He, X L.]]
[[Category: He, X L.]]
[[Category: Martick, M M.]]
[[Category: Martick, M M.]]
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[[Category: allosteric activation]]
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[[Category: Allosteric activation]]
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[[Category: crystal structure]]
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[[Category: Crystal structure]]
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[[Category: hormone/receptor complex]]
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[[Category: Hormone/receptor complex]]
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[[Category: natriuretic peptide receptor]]
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[[Category: Natriuretic peptide receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:05:57 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:32:10 2008''
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Revision as of 18:05, 2 May 2008

Image:1jdp.gif

Template:STRUCTURE 1jdp

Crystal Structure of Hormone/Receptor Complex


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.

About this Structure

1JDP is a Protein complex structure of sequences from Homo sapiens. 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 Fri May 2 21:05:57 2008

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