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| | {{STRUCTURE_1k9c| PDB=1k9c | SCENE= }} | | {{STRUCTURE_1k9c| PDB=1k9c | SCENE= }} |
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| - | '''Solution Structure of Calreticulin P-domain subdomain (residues 189-261)'''
| + | ===Solution Structure of Calreticulin P-domain subdomain (residues 189-261)=== |
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| - | ==Overview==
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| - | Calreticulin (CRT) is an abundant, soluble molecular chaperone of the endoplasmic reticulum. Similar to its membrane-bound homolog calnexin (CNX), it is a lectin that promotes the folding of proteins carrying N-linked glycans. Both proteins cooperate with an associated co-chaperone, the thiol-disulfide oxidoreductase ERp57. This enzyme catalyzes the formation of disulfide bonds in CNX and CRT-bound glycoprotein substrates. Previously, we solved the NMR structure of the central proline-rich P-domain of CRT comprising residues 189-288. This structure shows an extended hairpin topology, with three short anti-parallel beta-sheets, three small hydrophobic clusters, and one helical turn at the tip of the hairpin. We further demonstrated that the residues 225-251 at the tip of the CRT P-domain are involved in direct contacts with ERp57. Here, we show that the CRT P-domain fragment CRT(221-256) constitutes an autonomous folding unit, and has a structure highly similar to that of the corresponding region in CRT(189-288). Of the 36 residues present in CRT(221-256), 32 form a well-structured core, making this fragment one of the smallest known natural sequences to form a stable non-helical fold in the absence of disulfide bonds or tightly bound metal ions. CRT(221-256) comprises all the residues of the intact P-domain that were shown to interact with ERp57. Isothermal titration microcalorimetry (ITC) now showed affinity of this fragment for ERp57 similar to that of the intact P-domain, demonstrating that CRT(221-256) may be used as a low molecular mass mimic of CRT for further investigations of the interaction with ERp57. We also solved the NMR structure of the 73-residue fragment CRT(189-261), in which the tip of the hairpin and the first beta-sheet are well structured, but the residues 189-213 are disordered, presumably due to lack of stabilizing interactions across the hairpin.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12270713}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12270713 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_12270713}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1K9C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9C OCA]. | + | 1K9C is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9C OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Wuthrich, K.]] | | [[Category: Wuthrich, K.]] |
| | [[Category: Hairpin]] | | [[Category: Hairpin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:27:55 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 09:58:59 2008'' |
Revision as of 06:59, 2 July 2008
Template:STRUCTURE 1k9c
Solution Structure of Calreticulin P-domain subdomain (residues 189-261)
Template:ABSTRACT PUBMED 12270713
About this Structure
1K9C is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.
Reference
NMR structures of 36 and 73-residue fragments of the calreticulin P-domain., Ellgaard L, Bettendorff P, Braun D, Herrmann T, Fiorito F, Jelesarov I, Guntert P, Helenius A, Wuthrich K, J Mol Biol. 2002 Sep 27;322(4):773-84. PMID:12270713
Page seeded by OCA on Wed Jul 2 09:58:59 2008
