1icf: Difference between revisions
New page: left|200px<br /> <applet load="1icf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1icf, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF... |
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'''CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L'''<br /> | '''CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1ICF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NAG as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cathepsin_L Cathepsin L], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.15 3.4.22.15] Full crystallographic information is available from [http:// | 1ICF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Cathepsin_L Cathepsin L], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.15 3.4.22.15] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ICF OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: thyroglobulin type-1 domain]] | [[Category: thyroglobulin type-1 domain]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:00:57 2008'' | ||
Revision as of 17:00, 15 February 2008
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CRYSTAL STRUCTURE OF MHC CLASS II ASSOCIATED P41 II FRAGMENT IN COMPLEX WITH CATHEPSIN L
OverviewOverview
The lysosomal cysteine proteases cathepsins S and L play crucial roles in, the degradation of the invariant chain during maturation of MHC class II, molecules and antigen processing. The p41 form of the invariant chain, includes a fragment which specifically inhibits cathepsin L but not S. The, crystal structure of the p41 fragment, a homologue of the thyroglobulin, type-1 domains, has been determined at 2.0 A resolution in complex with, cathepsin L. The structure of the p41 fragment demonstrates a novel fold, consisting of two subdomains, each stabilized by disulfide bridges. The, first subdomain is an alpha-helix-beta-strand arrangement, whereas the, second subdomain has a predominantly beta-strand arrangement. The wedge, shape and three-loop arrangement of the p41 fragment bound to the active, site cleft of cathepsin L are reminiscent of the inhibitory edge of, cystatins, thus demonstrating the first example of convergent evolution, observed in cysteine protease inhibitors. However, the different fold of, the p41 fragment results in additional contacts with the top of the, R-domain of the enzymes, which defines the specificity-determining S2 and, S1' substrate-binding sites. This enables inhibitors based on the, thyroglobulin type-1 domain fold, in contrast to the rather non-selective, cystatins, to exhibit specificity for their target enzymes.
About this StructureAbout this Structure
1ICF is a Protein complex structure of sequences from Homo sapiens with as ligand. Active as Cathepsin L, with EC number 3.4.22.15 Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of MHC class II-associated p41 Ii fragment bound to cathepsin L reveals the structural basis for differentiation between cathepsins L and S., Guncar G, Pungercic G, Klemencic I, Turk V, Turk D, EMBO J. 1999 Feb 15;18(4):793-803. PMID:10022822
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