1r3c: Difference between revisions

Revision as of 14:22, 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:1r3c.png

Template:STRUCTURE 1r3c

THE STRUCTURE OF P38ALPHA C162S MUTANTTHE STRUCTURE OF P38ALPHA C162S MUTANT

Template:ABSTRACT PUBMED 14726206

About this StructureAbout this Structure

1R3C is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Lattice stabilization and enhanced diffraction in human p38 alpha crystals by protein engineering., Patel SB, Cameron PM, Frantz-Wattley B, O'Neill E, Becker JW, Scapin G, Biochim Biophys Acta. 2004 Jan 14;1696(1):67-73. PMID:14726206

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OCA

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-'''THE STRUCTURE OF P38ALPHA C162S MUTANT'''
+===THE STRUCTURE OF P38ALPHA C162S MUTANT===
-==Overview==
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-Mitogen-activated protein (MAP) kinase p38 alpha is activated in response to environmental stress and cytokines, and plays a significant role in inflammatory responses. For these reasons, it is an important target for the treatment of a wide range of inflammatory and autoimmune diseases. The crystals of p38 alpha that we obtained by published procedures were usually small, quite mosaic, and difficult to reproduce and thus posed a difficulty for the intensive high-resolution studies required for a structure-guided drug discovery approach. Based on crystallographic and biochemical evidences, we prepared a single point mutation of a surface cysteine (C162S) and found that it prevents aggregation and improves the homogeneity and stability of the enzyme. This mutation also facilitates the crystallization process and increases the diffracting power of p38 alpha crystals. Surprisingly, we found that the mutation induces a change in the conformation of a nearby surface loop resulting in stronger lattice interactions, consistent with the improved crystal quality. The mutant protein, because of its improved stability and strengthened lattice interactions, thus provides a significantly improved reagent for use in structure-based drug design for this important disease target.
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 [[Category: Serine/threonine kinase]]
 [[Category: Stabilization]]
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