1qli
From Proteopedia
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[[Category: metal-binding protein]] | [[Category: metal-binding protein]] | ||
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Revision as of 13:56, 30 October 2007
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QUAIL CYSTEINE AND GLYCINE-RICH PROTEIN, NMR, MINIMIZED AVERAGE STRUCTURE
Overview
Proteins of the cysteine-rich protein (CRP) family (CRP1, CRP2, and CRP3), are implicated in diverse processes linked to cellular differentiation and, growth control. CRP proteins contain two LIM domains, each formed by two, zinc-binding modules of the CCHC and CCCC type, respectively. The solution, structure of the carboxyl-terminal LIM domain (LIM2) from recombinant, quail CRP2 was determined by multidimensional homo- and heteronuclear, magnetic resonance spectroscopy. The folding topology retains both, independent zinc binding modules (CCHC and CCCC). Each module consists of, two orthogonally arranged antiparallel beta-sheets, and the, carboxyl-terminal CCCC module is terminated by an alpha-helix. 15N, magnetic relaxation data indicate that the modules differ in terms of, ... [(full description)]
About this Structure
1QLI is a [Single protein] structure of sequence from [Coturnix japonica] with ZN as [ligand]. Structure known Active Sites: ZN1 and ZN2. Full crystallographic information is available from [OCA].
Reference
Solution structure of the carboxyl-terminal LIM domain from quail cysteine-rich protein CRP2., Konrat R, Weiskirchen R, Krautler B, Bister K, J Biol Chem. 1997 May 2;272(18):12001-7. PMID:9115265
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