1dfp
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(New page: 200px<br /> <applet load="1dfp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dfp, resolution 2.4Å" /> '''FACTOR D INHIBITED B...)
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Revision as of 16:49, 29 October 2007
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FACTOR D INHIBITED BY DIISOPROPYL FLUOROPHOSPHATE
Overview
Factor D (D) is a serine protease, crucial for the activation of the, alternative complement pathway. Only a limited number of general serine, protease inhibitors are known to inhibit D, most of which covalently bind, to the serine hydroxyl of the catalytic triad. The structure of the first, enzyme:inhibitor covalent adduct of D with diisopropyl fluorophosphate, (DIP:D) to a resolution of 2.4 A is described. The inhibited enzyme is, similar in overall structure to the native enzyme and to trypsin, yet, exhibits notable differences in the active site. One region of the active, site is conserved between D and trypsin with respect to amino-acid, sequence and to conformation. Another reflects the amino-acid, substitutions and conformational flexibility between these enzymes. The, active-site ... [(full description)]
About this Structure
1DFP is a [Single protein] structure of sequence from [Homo sapiens] with DFP as [ligand]. Active as [[1]], with EC number [3.4.21.46]. Full crystallographic information is available from [OCA].
Reference
Structure of diisopropyl fluorophosphate-inhibited factor D., Cole LB, Chu N, Kilpatrick JM, Volanakis JE, Narayana SV, Babu YS, Acta Crystallogr D Biol Crystallogr. 1997 Mar 1;53(Pt 2):143-50. PMID:15299948
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