2j5h

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(New page: 200px<br /><applet load="2j5h" size="450" color="white" frame="true" align="right" spinBox="true" caption="2j5h" /> '''NMR ANALYSIS OF MOUSE CRIPTO CFC DOMAIN'''<b...)
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Revision as of 10:25, 21 November 2007


2j5h

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NMR ANALYSIS OF MOUSE CRIPTO CFC DOMAIN

Overview

We report here for the first time the solution structures at pH 3 and pH 6, of the synthetic CFC domain of mouse Cripto and of the point mutated, variant W107A that is unable to bind to the Alk4 Cripto receptor. NMR data, confirm that the CFC domain has a C1-C4, C2-C6, C3-C5 disulfide pattern, and show that structures are rather flexible and globally extended, with, three noncanonical antiparallel strands. His104 and Trp107 side chains, protrude from a protein edge and are strongly exposed to solvent, supporting previous evidence of direct involvement in receptor binding. On, the opposite molecule side, several nonpolar residues are gathered, forming a large hydrophobic patch that supposedly acts as interface with, the cell membrane or the adjacent EGF-like domain. A second hydrophilic, patch surrounding His104 and Trp107 is present only in the wild type, variant, suggesting a possible involvement in modulating Alk4 recognition.

About this Structure

2J5H is a Single protein structure of sequence from [1] with ACE and NH2 as ligands. Full crystallographic information is available from OCA.

Reference

Solution structure of mouse Cripto CFC domain and its inactive variant Trp107Ala., Calvanese L, Saporito A, Marasco D, D'Auria G, Minchiotti G, Pedone C, Paolillo L, Falcigno L, Ruvo M, J Med Chem. 2006 Nov 30;49(24):7054-62. PMID:17125258

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