1yk0
From Proteopedia
(New page: 200px<br /> <applet load="1yk0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yk0, resolution 2.4Å" /> '''structure of natriur...) |
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| - | [[Image:1yk0.gif|left|200px]]<br /> | + | [[Image:1yk0.gif|left|200px]]<br /><applet load="1yk0" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1yk0" size=" | + | |
caption="1yk0, resolution 2.4Å" /> | caption="1yk0, resolution 2.4Å" /> | ||
'''structure of natriuretic peptide receptor-C complexed with atrial natriuretic peptide'''<br /> | '''structure of natriuretic peptide receptor-C complexed with atrial natriuretic peptide'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Cardiovascular homeostasis and blood pressure regulation are reliant, in | + | 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. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1YK0 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 CL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1YK0 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=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YK0 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
| - | [[Category: Garcia, K | + | [[Category: Garcia, K C.]] |
[[Category: He, X.]] | [[Category: He, X.]] | ||
[[Category: CL]] | [[Category: CL]] | ||
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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 16:06:08 2008'' |
Revision as of 14:06, 21 February 2008
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structure of natriuretic peptide receptor-C complexed with atrial natriuretic peptide
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Acromesomelic dysplasia, Maroteaux type OMIM:[108961], Hypertension, salt-resistant (1) OMIM:[108962]
About this Structure
1YK0 is a Protein complex structure of sequences from Homo sapiens with and as ligands. 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
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