1anp
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(New page: 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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Revision as of 13:53, 12 November 2007
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SOLUTION CONFORMATION OF AN ATRIAL NATRIURETIC PEPTIDE VARIANT SELECTIVE FOR THE TYPE-A RECEPTOR
Contents |
Overview
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
Known disease associated with this structure: Acromesomelic dysplasia, Maroteaux type OMIM:[108961]
About this Structure
1ANP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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