4ju5: Difference between revisions

Line 1:

~~'''Unreleased~~ structure'''

===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase===

~~The entry 4ju5 is ON HOLD~~ ~~until Paper Publication~~

==Function==

[[http://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN]] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref>

~~Authors~~: ~~Bastos-Aristizabal, S~~.~~, Kozlov, G~~.~~, Gehring, K~~.

==About this Structure==

[[4ju5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JU5 OCA].

~~Description~~: ~~Crystal structure of the dimeric form of the bb' domains of human protein~~ disulfide isomerase

==Reference==

[[Category: Protein disulfide-isomerase]]

[[Category: Bastos-Aristizabal, S.]]

[[Category: Gehring, K.]]

[[Category: Kozlov, G.]]

[[Category: Chaperone]]

[[Category: Disulfide isomerase]]

[[Category: Isomerase]]

[[Category: Thioredoxin-like fold]]

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
+{{STRUCTURE_4ju5|  PDB=4ju5  |  SCENE=  }}
+===Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase===
-The entry 4ju5 is ON HOLD  until Paper Publication
+==Function==
+[[http://www.uniprot.org/uniprot/PDIA1_HUMAN PDIA1_HUMAN]] This multifunctional protein catalyzes the formation, breakage and rearrangement of disulfide bonds. At the cell surface, seems to act as a reductase that cleaves disulfide bonds of proteins attached to the cell. May therefore cause structural modifications of exofacial proteins. Inside the cell, seems to form/rearrange disulfide bonds of nascent proteins. At high concentrations, functions as a chaperone that inhibits aggregation of misfolded proteins. At low concentrations, facilitates aggregation (anti-chaperone activity). May be involved with other chaperones in the structural modification of the TG precursor in hormone biogenesis. Also acts a structural subunit of various enzymes such as prolyl 4-hydroxylase and microsomal triacylglycerol transfer protein MTTP.<ref>PMID:10636893</ref> <ref>PMID:12485997</ref>
-Authors: Bastos-Aristizabal, S., Kozlov, G., Gehring, K.
+==About this Structure==
+[[4ju5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4JU5 OCA].
-Description: Crystal structure of the dimeric form of the bb' domains of human protein disulfide isomerase
+==Reference==
+<references group="xtra"/><references/>
+[[Category: Protein disulfide-isomerase]]
+[[Category: Bastos-Aristizabal, S.]]
+[[Category: Gehring, K.]]
+[[Category: Kozlov, G.]]
+[[Category: Chaperone]]
+[[Category: Disulfide isomerase]]
+[[Category: Isomerase]]
+[[Category: Thioredoxin-like fold]]