1sa8: Difference between revisions

Revision as of 16:22, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1sa8.png

Template:STRUCTURE 1sa8

THE NMR STRUCTURE OF A STABLE AND COMPACT ALL-beta-SHEET VARIANT OF INTESTINAL FATTY ACID-BINDING PROTEINTHE NMR STRUCTURE OF A STABLE AND COMPACT ALL-beta-SHEET VARIANT OF INTESTINAL FATTY ACID-BINDING PROTEIN

Template:ABSTRACT PUBMED 15096629

About this StructureAbout this Structure

1SA8 is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.

ReferenceReference

The NMR structure of a stable and compact all-beta-sheet variant of intestinal fatty acid-binding protein., Ogbay B, Dekoster GT, Cistola DP, Protein Sci. 2004 May;13(5):1227-37. PMID:15096629

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-[[Image:1sa8.gif|left|200px]]
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-'''THE NMR STRUCTURE OF A STABLE AND COMPACT ALL-beta-SHEET VARIANT OF INTESTINAL FATTY ACID-BINDING PROTEIN'''
+===THE NMR STRUCTURE OF A STABLE AND COMPACT ALL-beta-SHEET VARIANT OF INTESTINAL FATTY ACID-BINDING PROTEIN===
-==Overview==
+<!--
-Intestinal fatty acid-binding protein (I-FABP) has a clam-shaped structure that may serve as a scaffold for the design of artificial enzymes and drug carriers. In an attempt to optimize the scaffold for increased access to the interior-binding cavity, several helix-less variants of I-FABP have been engineered. The solution-state NMR structure of the first generation helix-less variant, known as Delta17-SG, revealed a larger-than-expected and structurally ill-defined loop flanking the deletion site. We hypothesized that the presence of this loop, on balance, was energetically unfavorable for the stability of the protein. The structure exhibited no favorable pairwise or nonpolar interactions in the loop that could offset the loss of configurational entropy associated with the folding of this region of the protein. As an attempt to generate a more stable protein, we engineered a second-generation helix-less variant of I-FABP (Delta27-GG) by deleting 27 contiguous residues of the wild-type protein and replacing them with a G-G linker. The deletion site of this variant (D9 through N35) includes the 10 residues spanning the unstructured loop of Delta17-SG. Chemical denaturation experiments using steady-state fluorescence spectroscopy showed that the second-generation helix-less variant is energetically more stable than Delta17-SG. The three-dimensional structure of apo-Delta27-GG was solved using triple-resonance NMR spectroscopy along with the structure calculation and refinement protocols contained in the program package ARIA/CNS. In spite of the deletion of 27 residues, the structure assumes a compact all-beta-sheet fold with no unstructured loops and open access to the interior cavity.
+The line below this paragraph, {{ABSTRACT_PUBMED_15096629}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15096629 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15096629}}
 ==About this Structure==
-SA8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SA8 OCA].
+SA8 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SA8 OCA].
 ==Reference==
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 [[Category: Protein stability]]
 [[Category: Protein structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 08:28:36 2008''
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