1hhn
From Proteopedia
(New page: 200px<br /><applet load="1hhn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hhn" /> '''CALRETICULIN P-DOMAIN'''<br /> ==Overview==...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1hhn.gif|left|200px]]<br /><applet load="1hhn" size=" | + | [[Image:1hhn.gif|left|200px]]<br /><applet load="1hhn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1hhn" /> | caption="1hhn" /> | ||
'''CALRETICULIN P-DOMAIN'''<br /> | '''CALRETICULIN P-DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The NMR structure of the rat calreticulin P-domain, comprising residues | + | The NMR structure of the rat calreticulin P-domain, comprising residues 189-288, CRT(189-288), shows a hairpin fold that involves the entire polypeptide chain, has the two chain ends in close spatial proximity, and does not fold back on itself. This globally extended structure is stabilized by three antiparallel beta-sheets, with the beta-strands comprising the residues 189-192 and 276-279, 206-209 and 262-265, and 223-226 and 248-251, respectively. The hairpin loop of residues 227-247 and the two connecting regions between the beta-sheets contain a hydrophobic cluster, where each of the three clusters includes two highly conserved tryptophyl residues, one from each strand of the hairpin. The three beta-sheets and the three hydrophobic clusters form a repeating pattern of interactions across the hairpin that reflects the periodicity of the amino acid sequence, which consists of three 17-residue repeats followed by three 14-residue repeats. Within the global hairpin fold there are two well-ordered subdomains comprising the residues 219-258, and 189-209 and 262-284, respectively. These are separated by a poorly ordered linker region, so that the relative orientation of the two subdomains cannot be precisely described. The structure type observed for CRT(189-288) provides an additional basis for functional studies of the abundant endoplasmic reticulum chaperone calreticulin. |
==About this Structure== | ==About this Structure== | ||
| - | 1HHN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1HHN is a [http://en.wikipedia.org/wiki/Single_protein 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=1HHN OCA]. |
==Reference== | ==Reference== | ||
| Line 22: | Line 22: | ||
[[Category: molecular chaperone]] | [[Category: molecular chaperone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:18 2008'' |
Revision as of 11:01, 21 February 2008
|
CALRETICULIN P-DOMAIN
Overview
The NMR structure of the rat calreticulin P-domain, comprising residues 189-288, CRT(189-288), shows a hairpin fold that involves the entire polypeptide chain, has the two chain ends in close spatial proximity, and does not fold back on itself. This globally extended structure is stabilized by three antiparallel beta-sheets, with the beta-strands comprising the residues 189-192 and 276-279, 206-209 and 262-265, and 223-226 and 248-251, respectively. The hairpin loop of residues 227-247 and the two connecting regions between the beta-sheets contain a hydrophobic cluster, where each of the three clusters includes two highly conserved tryptophyl residues, one from each strand of the hairpin. The three beta-sheets and the three hydrophobic clusters form a repeating pattern of interactions across the hairpin that reflects the periodicity of the amino acid sequence, which consists of three 17-residue repeats followed by three 14-residue repeats. Within the global hairpin fold there are two well-ordered subdomains comprising the residues 219-258, and 189-209 and 262-284, respectively. These are separated by a poorly ordered linker region, so that the relative orientation of the two subdomains cannot be precisely described. The structure type observed for CRT(189-288) provides an additional basis for functional studies of the abundant endoplasmic reticulum chaperone calreticulin.
About this Structure
1HHN is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
NMR structure of the calreticulin P-domain., Ellgaard L, Riek R, Herrmann T, Guntert P, Braun D, Helenius A, Wuthrich K, Proc Natl Acad Sci U S A. 2001 Mar 13;98(6):3133-8. Epub 2001 Mar 6. PMID:11248044
Page seeded by OCA on Thu Feb 21 13:01:18 2008
