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1k9c

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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)'''
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===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.
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{{ABSTRACT_PUBMED_12270713}}
==About this Structure==
==About this Structure==
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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].
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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].
==Reference==
==Reference==
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[[Category: Wuthrich, K.]]
[[Category: Wuthrich, K.]]
[[Category: Hairpin]]
[[Category: Hairpin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:27:55 2008''
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''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

Image:1k9c.png

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

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