1anp: Difference between revisions
New page: left|200px<br /> <applet load="1anp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1anp" /> '''SOLUTION CONFORMATION OF AN ATRIAL NATRIURE... |
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'''SOLUTION CONFORMATION OF AN ATRIAL NATRIURETIC PEPTIDE VARIANT SELECTIVE FOR THE TYPE-A RECEPTOR'''<br /> | '''SOLUTION CONFORMATION OF AN ATRIAL NATRIURETIC PEPTIDE VARIANT SELECTIVE FOR THE TYPE-A RECEPTOR'''<br /> | ||
==Overview== | ==Overview== | ||
Two-dimensional NMR spectroscopy has been used to characterize the | Two-dimensional NMR spectroscopy has been used to characterize the solution conformation of an atrial natriuretic peptide (ANP) variant which is selective for the human natriuretic peptide receptor A (NPR-A) relative to receptor C (NPR-C). The ANP mutant, containing six substitutions, has reduced flexibility in aqueous solution relative to wild-type ANP and allows the observation of sufficient NOE connectivities for structure determination by distance geometry and restrained molecular dynamics calculations. The solution conformation is reasonably well defined, having an average backbone atom rms deviation from the average coordinates of approximately 1.1 A for residues 7-27. The structure is consistent with available functional data and shows a spatial separation between known receptor binding determinants and residues found to be outside the hormone-receptor interface. | ||
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
1ANP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1ANP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ANP OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Cunningham, B | [[Category: Cunningham, B C.]] | ||
[[Category: Fairbrother, W | [[Category: Fairbrother, W J.]] | ||
[[Category: Mcdowell, R | [[Category: Mcdowell, R S.]] | ||
[[Category: hypotensive hormone]] | [[Category: hypotensive hormone]] | ||
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Revision as of 12:46, 21 February 2008
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SOLUTION CONFORMATION OF AN ATRIAL NATRIURETIC PEPTIDE VARIANT SELECTIVE FOR THE TYPE-A RECEPTOR
OverviewOverview
Two-dimensional NMR spectroscopy has been used to characterize the solution conformation of an atrial natriuretic peptide (ANP) variant which is selective for the human natriuretic peptide receptor A (NPR-A) relative to receptor C (NPR-C). The ANP mutant, containing six substitutions, has reduced flexibility in aqueous solution relative to wild-type ANP and allows the observation of sufficient NOE connectivities for structure determination by distance geometry and restrained molecular dynamics calculations. The solution conformation is reasonably well defined, having an average backbone atom rms deviation from the average coordinates of approximately 1.1 A for residues 7-27. The structure is consistent with available functional data and shows a spatial separation between known receptor binding determinants and residues found to be outside the hormone-receptor interface.
DiseaseDisease
Known disease associated with this structure: Acromesomelic dysplasia, Maroteaux type OMIM:[108961]
About this StructureAbout this Structure
1ANP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Solution conformation of an atrial natriuretic peptide variant selective for the type A receptor., Fairbrother WJ, McDowell RS, Cunningham BC, Biochemistry. 1994 Aug 2;33(30):8897-904. PMID:8043577
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