1vyo

From Proteopedia

(Difference between revisions)

Revision as of 13:08, 13 December 2023

Crystal structure of avidin

Structural highlights

1vyo is a 2 chain structure with sequence from Gallus gallus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 1.48Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

AVID_CHICK The biological function of avidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of avidin).

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

The chicken genome encodes several biotin-binding proteins, including avidin and avidin-related protein 4 (AVR4). In addition to D-biotin, avidin binds an azo dye compound, 4-hydroxyazobenzene-2-carboxylic acid (HABA), but the HABA-binding properties of AVR4 are not yet known. Differential scanning calorimetry, UV/visible spectroscopy, and molecular modeling were used to analyze the binding of 15 azo molecules to avidin and AVR4. Significant differences are seen in azo compound preferences for the two proteins, emphasizing the importance of the loop between strands beta3 and beta4 for azo ligand recognition; information on these loops is provided by the high-resolution (1.5 A) X-ray structure for avidin reported here. These results may be valuable in designing improved tools for avidin-based life science and nanobiotechnology applications.

Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4.,Repo S, Paldanius TA, Hytonen VP, Nyholm TK, Halling KK, Huuskonen J, Pentikainen OT, Rissanen K, Slotte JP, Airenne TT, Salminen TA, Kulomaa MS, Johnson MS Chem Biol. 2006 Oct;13(10):1029-39. PMID:17052607^[1]

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

References

↑ Repo S, Paldanius TA, Hytonen VP, Nyholm TK, Halling KK, Huuskonen J, Pentikainen OT, Rissanen K, Slotte JP, Airenne TT, Salminen TA, Kulomaa MS, Johnson MS. Binding properties of HABA-type azo derivatives to avidin and avidin-related protein 4. Chem Biol. 2006 Oct;13(10):1029-39. PMID:17052607 doi:10.1016/j.chembiol.2006.08.006

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

Categories: Gallus gallus | Large Structures | Airenne TT | Johnson MS | Salminen TA

@@ Line 3: / Line 3: @@
 <StructureSection load='1vyo' size='340' side='right'caption='[[1vyo]], [[Resolution|resolution]] 1.48&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1vyo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chick Chick]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VYO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1vyo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VYO FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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]] 1.48&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1avd|1avd]], [[1ave|1ave]], [[1ij8|1ij8]], [[1ldo|1ldo]], [[1ldq|1ldq]], [[1lel|1lel]], [[1nqn|1nqn]], [[1rav|1rav]], [[2avi|2avi]], [[2cam|2cam]]</div></td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></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=1vyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vyo OCA], [https://pdbe.org/1vyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1vyo RCSB], [https://www.ebi.ac.uk/pdbsum/1vyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1vyo ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/AVID_CHICK AVID_CHICK]] The biological function of avidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of avidin).
+[https://www.uniprot.org/uniprot/AVID_CHICK AVID_CHICK] The biological function of avidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of avidin).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 36: / Line 36: @@
 __TOC__
 </StructureSection>
-[[Category: Chick]]
+[[Category: Gallus gallus]]
 [[Category: Large Structures]]
-[[Category: Airenne, T T]]
+[[Category: Airenne TT]]
-[[Category: Johnson, M S]]
+[[Category: Johnson MS]]
-[[Category: Salminen, T A]]
+[[Category: Salminen TA]]
-[[Category: Biotin]]
-[[Category: Glycoprotein]]

1vyo

From Proteopedia

Revision as of 13:08, 13 December 2023

Crystal structure of avidin

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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