2c0e: Difference between revisions

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[[Image:2c0e.~~gif~~|left|200px]]

[[Image:2c0e.png|left|200px]]

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~~'''~~STRUCTURE OF PDI-RELATED CHAPERONE, WIND WITH HIS-TAG ON C-TERMINUS.~~'''~~

===STRUCTURE OF PDI-RELATED CHAPERONE, WIND WITH HIS-TAG ON C-TERMINUS.===

~~==Overview==~~

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The ~~structures of the PDI-related protein Wind (with a C-terminal His(6) tag) and the mutants Y53S~~, ~~Y53F and Y55K have been determined and compared with~~ the ~~wild-type structure with~~ the ~~His~~(~~6) tag~~ at ~~the N-terminus~~. All five structures show the same mode of dimerization, showing that this was not an artefact introduced by the nearby N-terminal His(6) tag and suggesting that this dimer may also be the biologically active form. ~~Although the mutants Y53S and Y55K completely abrogate transport of the protein Pipe (which appears to be the primary function of Wind in the cell~~), ~~only subtle differences can be seen in~~ the ~~putative Pipe~~-binding region. The Pipe binding in the active forms appears to involve hydrophobic interactions between aromatic systems, whereas the inactive mutants may be able to bind more strongly with the help of hydrogen bonds, which could disturb the delicate equilibrium required for effective Pipe transport.

The line below this paragraph, {{ABSTRACT_PUBMED_16699185}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 16699185 is the PubMed ID number.

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==About this Structure==

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[[Category: Wind mutant]]

[[Category: Windbeutel]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 21~~:03:09 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:43:58 2008''

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-[[Image:2c0e.gif|left|200px]]
+{{Seed}}
+[[Image:2c0e.png|left|200px]]
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 {{STRUCTURE_2c0e|  PDB=2c0e  |  SCENE=  }}
-'''STRUCTURE OF PDI-RELATED CHAPERONE, WIND WITH HIS-TAG ON C-TERMINUS.'''
+===STRUCTURE OF PDI-RELATED CHAPERONE, WIND WITH HIS-TAG ON C-TERMINUS.===
-==Overview==
+<!--
-The structures of the PDI-related protein Wind (with a C-terminal His(6) tag) and the mutants Y53S, Y53F and Y55K have been determined and compared with the wild-type structure with the His(6) tag at the N-terminus. All five structures show the same mode of dimerization, showing that this was not an artefact introduced by the nearby N-terminal His(6) tag and suggesting that this dimer may also be the biologically active form. Although the mutants Y53S and Y55K completely abrogate transport of the protein Pipe (which appears to be the primary function of Wind in the cell), only subtle differences can be seen in the putative Pipe-binding region. The Pipe binding in the active forms appears to involve hydrophobic interactions between aromatic systems, whereas the inactive mutants may be able to bind more strongly with the help of hydrogen bonds, which could disturb the delicate equilibrium required for effective Pipe transport.
+The line below this paragraph, {{ABSTRACT_PUBMED_16699185}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16699185 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16699185}}
 ==About this Structure==
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 [[Category: Wind mutant]]
 [[Category: Windbeutel]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 21:03:09 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:43:58 2008''