1dfj

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Revision as of 14:07, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="1dfj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dfj, resolution 2.5Å" /> '''RIBONUCLEASE INHIBITO...)
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File:1dfj.jpg


1dfj, resolution 2.5Å

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RIBONUCLEASE INHIBITOR COMPLEXED WITH RIBONUCLEASE A

OverviewOverview

The leucine-rich repeat is a recently characterized structural motif used, in molecular recognition processes as diverse as signal transduction, cell, adhesion, cell development, DNA repair and RNA processing. We present here, the crystal structure at 2.5 A resolution of the complex between, ribonuclease A and ribonuclease inhibitor, a protein built entirely of, leucine-rich repeats. The unusual non-globular structure of ribonuclease, inhibitor, its solvent-exposed parallel beta-sheet and the conformational, flexibility of the structure are used in the interaction; they appear to, be the principal reasons for the effectiveness of leucine-rich repeats as, protein-binding motifs. The structure can serve as a model for the, interactions of other proteins containing leucine-rich repeats with their, ligands.

About this StructureAbout this Structure

1DFJ is a Protein complex structure of sequences from Bos taurus and Sus scrofa with SO4 and ACE as ligands. Active as Pancreatic ribonuclease, with EC number 3.1.27.5 Full crystallographic information is available from OCA.

ReferenceReference

A structural basis of the interactions between leucine-rich repeats and protein ligands., Kobe B, Deisenhofer J, Nature. 1995 Mar 9;374(6518):183-6. PMID:7877692

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