1mek
From Proteopedia
(New page: 200px<br /> <applet load="1mek" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mek" /> '''HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 ...) |
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'''HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES'''<br /> | '''HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES'''<br /> | ||
==Overview== | ==Overview== | ||
| - | As a first step in dissecting the structure of human protein disulfide | + | As a first step in dissecting the structure of human protein disulfide isomerase (PDI), the structure of a fragment corresponding to the first 120 residues of its sequence has been determined using heteronuclear multidimensional NMR techniques. As expected from its primary structure homology, the fragment has the thioredoxin fold. Similarities and differences in their structures help to explain why thioredoxins are reductants, whereas PDI is an oxidant of protein thiol groups. The results confirm that PDI has a modular, multidomain structure, which will facilitate its structural and functional characterization. |
==About this Structure== | ==About this Structure== | ||
| - | 1MEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] Full crystallographic information is available from [http:// | + | 1MEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Protein_disulfide-isomerase Protein disulfide-isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.3.4.1 5.3.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MEK OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein disulfide-isomerase]] | [[Category: Protein disulfide-isomerase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Creighton, T | + | [[Category: Creighton, T E.]] |
| - | [[Category: Darby, N | + | [[Category: Darby, N J.]] |
[[Category: Dijkstra, K.]] | [[Category: Dijkstra, K.]] | ||
[[Category: Kemmink, J.]] | [[Category: Kemmink, J.]] | ||
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[[Category: redox-active center]] | [[Category: redox-active center]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:54:33 2008'' |
Revision as of 11:54, 21 February 2008
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HUMAN PROTEIN DISULFIDE ISOMERASE, NMR, 40 STRUCTURES
Overview
As a first step in dissecting the structure of human protein disulfide isomerase (PDI), the structure of a fragment corresponding to the first 120 residues of its sequence has been determined using heteronuclear multidimensional NMR techniques. As expected from its primary structure homology, the fragment has the thioredoxin fold. Similarities and differences in their structures help to explain why thioredoxins are reductants, whereas PDI is an oxidant of protein thiol groups. The results confirm that PDI has a modular, multidomain structure, which will facilitate its structural and functional characterization.
About this Structure
1MEK 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
Structure determination of the N-terminal thioredoxin-like domain of protein disulfide isomerase using multidimensional heteronuclear 13C/15N NMR spectroscopy., Kemmink J, Darby NJ, Dijkstra K, Nilges M, Creighton TE, Biochemistry. 1996 Jun 18;35(24):7684-91. PMID:8672469
Page seeded by OCA on Thu Feb 21 13:54:33 2008
