1f2r
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(New page: 200px<br /><applet load="1f2r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f2r" /> '''NMR STRUCTURE OF THE HETERODIMERIC COMPLEX B...)
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Revision as of 12:26, 20 November 2007
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NMR STRUCTURE OF THE HETERODIMERIC COMPLEX BETWEEN CAD DOMAINS OF CAD AND ICAD
Overview
We present here the structure of the complex between the CAD domain of, caspase activated deoxyribonuclease (CAD) and the CAD domain of its, inhibitor (ICAD), determined by nuclear magnetic resonance spectroscopy., The two domains adopt a very similar fold, which consists of an, alpha-helix and a beta-sheet, and are aligned side by side in the complex., Notably, the positive charges on the strand beta2 at one end of the, beta-sheet of CAD and negative charges around the opposite end of the, beta-sheet of ICAD are paired in the complex. Point mutations of the, charged amino acids at this interface, on either CAD or ICAD, prevented, formation of the functional CAD-ICAD complex. This implies that the, interaction between the CAD domains of CAD and ICAD is an essential step, in the correct folding of CAD in the complex.
About this Structure
1F2R is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Structure of the heterodimeric complex between CAD domains of CAD and ICAD., Otomo T, Sakahira H, Uegaki K, Nagata S, Yamazaki T, Nat Struct Biol. 2000 Aug;7(8):658-62. PMID:10932250
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