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| - | [[Image:1h0p.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1h0p| PDB=1h0p | SCENE= }} | | {{STRUCTURE_1h0p| PDB=1h0p | SCENE= }} |
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| - | '''CYCLOPHILIN_5 FROM C. ELEGANS'''
| + | ===CYCLOPHILIN_5 FROM C. ELEGANS=== |
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| - | ==Overview==
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| - | The free-living nematode Caenorhabditis elegans expresses 18 cyclophilin isoforms, eight of which are conserved single domain forms, comprising two closely related secreted or type B forms (CYP-5 and CYP-6). Recombinant CYP-5 has been purified, crystallised and the X-ray structure solved to a resolution of 1.75A. The detailed molecular architecture most strongly resembles the structure of human cyclophilin B with conserved changes in loop structure and N and C-terminal extensions. Interestingly, the active site pocket is occupied by a molecule of dithiothreitol though this has little effect on the geometry of the active site which is similar to other cyclophilin structures. The peptidyl-prolyl isomerase activity of CYP-5 has been characterised against the substrate N-succinyl-Ala-Ala-Pro-Phe-p-nitroanilide, and gives a k(cat)/K(m) value of 3.6x10(6)M(-1)s(-1) that compares with a value of 6.3x10(6)M(-1)s(-1) for human cyclophilin B. The immunosuppressive drug cyclosporin A binds and inhibits CYP-5 with an IC(50) value of 50nM, which is comparable to the value of 84nM found for human cyclophilin B. CYP-6 has 67% sequence identity with CYP-5 and a molecular model was built based on the CYP-5 crystal structure. The model shows that CYP-5 and CYP-6 are likely to have very similar structures, but with a markedly increased number of negative charges distributed around the surface of CYP-6. The spatial expression patterns of the cyclophilin B isoforms were examined using transgenic animals carrying a LacZ reporter fusion to these genes, and both cyp-5 and cyp-6 are found to be expressed in an overlapping fashion in the nematode gut. The temporal expression pattern of cyp-5 was further determined and revealed a constitutive expression pattern, with highest abundance levels being found in the embryo. | + | The line below this paragraph, {{ABSTRACT_PUBMED_12215411}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12215411 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12215411}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Isomerase]] | | [[Category: Isomerase]] |
| | [[Category: Rotamase]] | | [[Category: Rotamase]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:15:56 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 06:25:39 2008'' |
Revision as of 03:25, 1 July 2008
Template:STRUCTURE 1h0p
CYCLOPHILIN_5 FROM C. ELEGANS
Template:ABSTRACT PUBMED 12215411
About this Structure
1H0P is a Single protein structure of sequence from Caenorhabditis elegans. Full crystallographic information is available from OCA.
Reference
Structural and biological characterisation of the gut-associated cyclophilin B isoforms from Caenorhabditis elegans., Picken NC, Eschenlauer S, Taylor P, Page AP, Walkinshaw MD, J Mol Biol. 2002 Sep 6;322(1):15-25. PMID:12215411
Page seeded by OCA on Tue Jul 1 06:25:39 2008
