1bjx
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(New page: 200px<br /> <applet load="1bjx" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bjx" /> '''HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 ...)
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Revision as of 14:04, 12 November 2007
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HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 24 STRUCTURES
Overview
Protein disulfide isomerase (PDI) is a multifunctional protein of the, endoplasmic reticulum, which catalyzes the formation, breakage and, rearrangement of disulfide bonds during protein folding. It consists of, four domains designated a, b, b and a. Both a and a domains contains an, active site with the sequence motif -Cys-Gly-His-Cys-involved directly in, thiol-disulfide exchange reactions. As expected these domains have, structures very similar to the ubiquitous redox protein thioredoxin. A, low-resolution NMR structure of the b domain revealed that this domain, adopts a fold similar to the PDI a domain and thioredoxin [Kemmink, J., Darby, N.J., Dijkstra, K., Nilges, M. and Creighton, T.E. (1997) Curr., Biol. 7, 239-245]. A refined ensemble of solution structures based on the, input of 1865 structural restraints shows that the structure of PDI b is, well defined throughout the complete protein except for about 10 residues, at the C-terminus of the sequence. 15N relaxation data show that these, residues are disordered and not part of this structural domain. Therefore, the domain boundaries of PDI can now be fixed with reasonable precision., Structural comparison of the PDI b domain with thioredoxin and PDI a, reveals several features important for thiol-disulfide exchange activity.
About this Structure
1BJX is a Single protein structure of sequence from Homo sapiens. Active as Protein disulfide-isomerase, with EC number 5.3.4.1 Full crystallographic information is available from OCA.
Reference
The structure in solution of the b domain of protein disulfide isomerase., Kemmink J, Dijkstra K, Mariani M, Scheek RM, Penka E, Nilges M, Darby NJ, J Biomol NMR. 1999 Apr;13(4):357-68. PMID:10383197
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