This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1t1v

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 07:40, 22 September 2021

Crystal Structure of the Glutaredoxin-like Protein SH3BGRL3 at 1.6 A resolution

Structural highlights

1t1v is a 2 chain structure with sequence from Lk3 transgenic mice. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	, ,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SH3L3_MOUSE] Could act as a modulator of glutaredoxin biological activity (By similarity).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

We report the 1.6 Angstrom resolution crystal structure of SH3BGRL3, a member of a new mammalian protein family of unknown function. The observed "thioredoxin fold" of SH3BGRL3 matches the tertiary structure of glutaredoxins, even in the N-terminal region where the sequence similarity between the two protein families is negligible. In particular, SH3BGRL3 displays structural modifications at the N-terminal Cys-x-x-Cys loop, responsible for glutathione binding and catalysis in glutaredoxins. The loop hosts a six residue insertion, yielding an extra N-terminal-capped helical turn, first observed here for the thioredoxin fold. This, together with deletion of both Cys residues, results in a substantial reshaping of the neighboring cleft, where glutathione is hosted in glutaredoxins. While not active in redox reaction and glutathione binding, SH3BGRL3 may act as an endogenous modulator of glutaredoxin activities by competing, with its fully conserved thioredoxin fold, for binding to yet unknown target proteins.

Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution.,Nardini M, Mazzocco M, Massaro A, Maffei M, Vergano A, Donadini A, Scartezzini P, Bolognesi M Biochem Biophys Res Commun. 2004 May 28;318(2):470-6. PMID:15120624^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Nardini M, Mazzocco M, Massaro A, Maffei M, Vergano A, Donadini A, Scartezzini P, Bolognesi M. Crystal structure of the glutaredoxin-like protein SH3BGRL3 at 1.6 Angstrom resolution. Biochem Biophys Res Commun. 2004 May 28;318(2):470-6. PMID:15120624 doi:10.1016/j.bbrc.2004.04.050

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1t1v"

@@ Line 3: / Line 3: @@
 <StructureSection load='1t1v' size='340' side='right'caption='[[1t1v]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1t1v]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1T1V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1t1v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T1V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1T1V FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACY:ACETIC+ACID'>ACY</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1v OCA], [http://pdbe.org/1t1v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1t1v RCSB], [http://www.ebi.ac.uk/pdbsum/1t1v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1t1v ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1t1v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t1v OCA], [https://pdbe.org/1t1v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1t1v RCSB], [https://www.ebi.ac.uk/pdbsum/1t1v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1t1v ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SH3L3_MOUSE SH3L3_MOUSE]] Could act as a modulator of glutaredoxin biological activity (By similarity).
+[[https://www.uniprot.org/uniprot/SH3L3_MOUSE SH3L3_MOUSE]] Could act as a modulator of glutaredoxin biological activity (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1t1v

From Proteopedia

Revision as of 07:40, 22 September 2021

Crystal Structure of the Glutaredoxin-like Protein SH3BGRL3 at 1.6 A resolution

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox