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| - | [[Image:1z2m.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1z2m.png|left|200px]] |
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| | {{STRUCTURE_1z2m| PDB=1z2m | SCENE= }} | | {{STRUCTURE_1z2m| PDB=1z2m | SCENE= }} |
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| - | '''Crystal Structure of ISG15, the Interferon-Induced Ubiquitin Cross Reactive Protein'''
| + | ===Crystal Structure of ISG15, the Interferon-Induced Ubiquitin Cross Reactive Protein=== |
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| - | ==Overview==
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| - | The biological effects of the ISG15 protein arise in part from its conjugation to cellular targets as a primary response to interferon-alpha/beta induction and other markers of viral or parasitic infection. Recombinant full-length ISG15 has been produced for the first time in high yield by mutating Cys78 to stabilize the protein and by cloning in a C-terminal arginine cap to protect the C terminus against proteolytic inactivation. The cap is subsequently removed with carboxypeptidase B to yield mature biologically active ISG15 capable of stoichiometric ATP-dependent thiolester formation with its human UbE1L activating enzyme. The three-dimensional structure of recombinant ISG15C78S was determined at 2.4-A resolution. The ISG15 structure comprises two beta-grasp folds having main chain root mean square deviation (r.m.s.d.) values from ubiquitin of 1.7 A (N-terminal) and 1.0 A (C-terminal). The beta-grasp domains pack across two conserved 3(10) helices to bury 627 A2 that accounts for 7% of the total solvent-accessible surface area. The distribution of ISG15 surface charge forms a ridge of negative charge extending nearly the full-length of the molecule. Additionally, the N-terminal domain contains an apolar region comprising almost half its solvent accessible surface. The C-terminal domain of ISG15 was superimposed on the structure of Nedd8 (r.m.s.d. = 0.84 A) bound to its AppBp1-Uba3 activating enzyme to model ISG15 binding to UbE1L. The docking model predicts several key side-chain interactions that presumably define the specificity between the ubiquitin and ISG15 ligation pathways to maintain functional integrity of their signaling. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15917233}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15917233 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15917233}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Isg15]] | | [[Category: Isg15]] |
| | [[Category: Ubiquitin cross reactive protein]] | | [[Category: Ubiquitin cross reactive protein]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:06:42 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 13:34:17 2008'' |
Revision as of 10:34, 29 July 2008
Template:STRUCTURE 1z2m
Crystal Structure of ISG15, the Interferon-Induced Ubiquitin Cross Reactive Protein
Template:ABSTRACT PUBMED 15917233
About this Structure
1Z2M is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the interferon-induced ubiquitin-like protein ISG15., Narasimhan J, Wang M, Fu Z, Klein JM, Haas AL, Kim JJ, J Biol Chem. 2005 Jul 22;280(29):27356-65. Epub 2005 May 24. PMID:15917233
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