1apq

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Revision as of 22:25, 29 October 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="1apq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1apq" /> '''STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C...)
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1apq

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STRUCTURE OF THE EGF-LIKE MODULE OF HUMAN C1R, NMR, 19 STRUCTURES

OverviewOverview

The calcium-dependent interaction between C1r and C1s, the two homologous, serine proteases of the first component of human complement C1, is, mediated by their N-terminal regions. The latter comprise an epidermal, growth factor (EGF)-like module exhibiting the consensus sequence, characteristic of Ca(2+)-binding EGF modules, surrounded by two CUB, modules. Due to its Ca2+ binding ability, the C1r EGF-like module, (C1r-EGF) is supposed to participate in the C1r-C1s interaction. An, additional interesting feature of C1r-EGF is the unusually large loop, connecting the first two conserved cysteine residues. The solution, structure of synthetic C1r-EGF (residues 123-175) has been determined, using nuclear magnetic resonance and combined simulated, annealing-restrained molecular dynamics ... [(full description)]

About this StructureAbout this Structure

1APQ is a [Single protein] structure of sequence from [Homo sapiens]. Active as [[1]], with EC number [3.4.21.41]. Full crystallographic information is available from [OCA].

ReferenceReference

Solution structure of the epidermal growth factor (EGF)-like module of human complement protease C1r, an atypical member of the EGF family., Bersch B, Hernandez JF, Marion D, Arlaud GJ, Biochemistry. 1998 Feb 3;37(5):1204-14. PMID:9477945

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