1cf1

From Proteopedia

(Difference between revisions)

Current revision

ARRESTIN FROM BOVINE ROD OUTER SEGMENTS

Structural highlights

1cf1 is a 4 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.8Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

ARRS_BOVIN Note=S-antigen induces autoimmune uveitis.

Function

ARRS_BOVIN Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade.

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

G protein-coupled signaling is utilized by a wide variety of eukaryotes for communicating information from the extracellular environment. Signal termination is achieved by the action of the arrestins, which bind to activated, phosphorylated G protein-coupled receptors. We describe here crystallographic studies of visual arrestin in its basal conformation. The salient features of the structure are a bipartite molecule with an unusual polar core. This core is stabilized in part by an extended carboxy-terminal tail that locks the molecule into an inactive state. In addition, arrestin is found to be a dimer of two asymmetric molecules, suggesting an intrinsic conformational plasticity. In conjunction with biochemical and mutagenesis data, we propose a molecular mechanism by which arrestin is activated for receptor binding.

The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation.,Hirsch JA, Schubert C, Gurevich VV, Sigler PB Cell. 1999 Apr 16;97(2):257-69. PMID:10219246^[1]

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

References

↑ Hirsch JA, Schubert C, Gurevich VV, Sigler PB. The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation. Cell. 1999 Apr 16;97(2):257-69. PMID:10219246

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 See Also
7 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1cf1"

@@ Line 3: / Line 3: @@
 <StructureSection load='1cf1' size='340' side='right'caption='[[1cf1]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1cf1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CF1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1cf1]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CF1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CF1 FirstGlance]. <br>
-</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=1cf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cf1 OCA], [https://pdbe.org/1cf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cf1 RCSB], [https://www.ebi.ac.uk/pdbsum/1cf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cf1 ProSAT]</span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8&#8491;</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=1cf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cf1 OCA], [https://pdbe.org/1cf1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cf1 RCSB], [https://www.ebi.ac.uk/pdbsum/1cf1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cf1 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN]] Note=S-antigen induces autoimmune uveitis.
+[https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN] Note=S-antigen induces autoimmune uveitis.
 == Function ==
-[[https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN]] Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade.
+[https://www.uniprot.org/uniprot/ARRS_BOVIN ARRS_BOVIN] Arrestin is one of the major proteins of the ros (retinal rod outer segments); it binds to photoactivated-phosphorylated rhodopsin, thereby apparently preventing the transducin-mediated activation of phosphodiesterase. Isoform B plays a role in the phototransduction cascade.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 37: @@
 __TOC__
 </StructureSection>
-[[Category: Bovin]]
+[[Category: Bos taurus]]
 [[Category: Large Structures]]
-[[Category: Gurevich, V V]]
+[[Category: Gurevich VV]]
-[[Category: Hirsch, J A]]
+[[Category: Hirsch JA]]
-[[Category: Schubert, C]]
+[[Category: Schubert C]]
-[[Category: Sigler, P B]]
+[[Category: Sigler PB]]
-[[Category: Binding to acticated and phosphorylated rhodopsin]]
-[[Category: Desensitisation of the visual transduction cascade]]
-[[Category: Structural protein]]
-[[Category: Visual arrestin]]

1cf1

From Proteopedia

Current revision

ARRESTIN FROM BOVINE ROD OUTER SEGMENTS

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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