1jdn

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[[Image:1jdn.gif|left|200px]]
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{{STRUCTURE_1jdn| PDB=1jdn | SCENE= }}
{{STRUCTURE_1jdn| PDB=1jdn | SCENE= }}
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'''Crystal Structure of Hormone Receptor'''
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===Crystal Structure of Hormone Receptor===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 11533490 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11533490}}
==About this Structure==
==About this Structure==
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[[Category: Dimer]]
[[Category: Dimer]]
[[Category: Natriuretic peptide receptor]]
[[Category: Natriuretic peptide receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:05:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 20:05:00 2008''

Revision as of 17:05, 1 July 2008

Template:STRUCTURE 1jdn

Crystal Structure of Hormone Receptor

Template:ABSTRACT PUBMED 11533490

About this Structure

1JDN is a Single protein structure of sequence 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

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