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| - | [[Image:1yk0.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1yk0.png|left|200px]] |
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| | {{STRUCTURE_1yk0| PDB=1yk0 | SCENE= }} | | {{STRUCTURE_1yk0| PDB=1yk0 | SCENE= }} |
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| - | '''structure of natriuretic peptide receptor-C complexed with atrial natriuretic peptide'''
| + | ===structure of natriuretic peptide receptor-C complexed with atrial natriuretic peptide=== |
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| - | ==Overview==
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| - | Cardiovascular homeostasis and blood pressure regulation are reliant, in part, on interactions between natriuretic peptide (NP) hormones and natriuretic peptide receptors (NPR). The C-type NPR (NPR-C) is responsible for clearance of NP hormones from the circulation, and displays a cross-reactivity for all NP hormones (ANP, BNP, and CNP), in contrast to other NPRs, which are more restricted in their specificity. In order to elucidate the structural determinants for the binding specificity and cross-reactivity of NPR-C with NP hormones, we have determined the crystal structures of the complexes of NPR-C with atrial natriuretic peptide (ANP), and with brain natriuretic peptide (BNP). A structural comparison of these complexes, with the previous structure of the NPR-C/CNP complex, reveals that NPR-C uses a conformationally inflexible surface to bind three different, highly flexible, NP ligands. The complex structures support a mechanism of rigid promiscuity rather than conformational plasticity by the receptor. While ANP and BNP appear to adopt similar receptor-bound conformations, the CNP structure diverges, yet shares sets of common receptor contacts with the other ligands. The degenerate versus selective hormone recognition properties of different NPRs appears to derive largely from two cavities on the receptor surfaces, pocket I and pocket II, that serve as anchoring sites for hormone side-chains and modulate receptor selectivity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_16870210}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 16870210 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_16870210}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hormone/receptor complex]] | | [[Category: Hormone/receptor complex]] |
| | [[Category: Natriuretic peptide receptor]] | | [[Category: Natriuretic peptide receptor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:25:08 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:37:33 2008'' |
Revision as of 09:37, 10 July 2008
Template:STRUCTURE 1yk0
structure of natriuretic peptide receptor-C complexed with atrial natriuretic peptide
Template:ABSTRACT PUBMED 16870210
About this Structure
1YK0 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural determinants of natriuretic peptide receptor specificity and degeneracy., He XL, Dukkipati A, Garcia KC, J Mol Biol. 2006 Aug 25;361(4):698-714. Epub 2006 Jul 10. PMID:16870210
Page seeded by OCA on Thu Jul 10 12:37:33 2008
