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1bio
From Proteopedia
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HUMAN COMPLEMENT FACTOR D IN COMPLEX WITH ISATOIC ANHYDRIDE INHIBITOR
Overview
Factor D is a serine protease essential for the activation of the, alternative pathway of complement. The structures of native factor D and a, complex formed with isatoic anhydride inhibitor were determined at, resolution of 2.3 and 1.5 A, respectively, in an isomorphous monoclinic, crystal form containing one molecule per asymmetric unit. The native, structure was compared with structures determined previously in a, triclinic cell containing two molecules with different active site, conformations. The current structure shows greater similarity with, molecule B in the triclinic cell, suggesting that this may be the dominant, factor D conformation in solution. The major conformational differences, with molecule A in the triclinic cell are located in four regions, three, of which are close ... [(full description)]
About this Structure
1BIO is a [Single protein] structure of sequence from [Homo sapiens] with SOA and GOL as [ligands]. Active as [[1]], with EC number [3.4.21.46]. Full crystallographic information is available from [OCA].
Reference
Structures of native and complexed complement factor D: implications of the atypical His57 conformation and self-inhibitory loop in the regulation of specific serine protease activity., Jing H, Babu YS, Moore D, Kilpatrick JM, Liu XY, Volanakis JE, Narayana SV, J Mol Biol. 1998 Oct 9;282(5):1061-81. PMID:9753554
Page seeded by OCA on Mon Oct 29 21:48:30 2007
Categories: Homo sapiens | Single protein | Babu, Y.S. | Jing, H. | Kilpatrick, J.M. | Liu, X.Y. | Moore, D. | Narayana, S.V.L. | Volanakis, J.E. | GOL | SOA | Catalytic triad | Complement | Factor d | Hydrolase | Self-regulation | Serine protease
