3vhh: Difference between revisions

From Proteopedia
Jump to navigation Jump to search
No edit summary
No edit summary
 
(7 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:3vhh.jpg|left|200px]]


<!--
==Crystal structure of DiMe-biotin-avidin complex==
The line below this paragraph, containing "STRUCTURE_3vhh", creates the "Structure Box" on the page.
<StructureSection load='3vhh' size='340' side='right'caption='[[3vhh]], [[Resolution|resolution]] 2.26&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)  
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[3vhh]] is a 4 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=3VHH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3VHH FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.26&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=VHH:5-[(3AS,4S,6AR)-1,3-DIMETHYL-2-OXOHEXAHYDRO-1H-THIENO[3,4-D]IMIDAZOL-4-YL]PENTANOIC+ACID'>VHH</scene></td></tr>
{{STRUCTURE_3vhh|  PDB=3vhh  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3vhh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3vhh OCA], [https://pdbe.org/3vhh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3vhh RCSB], [https://www.ebi.ac.uk/pdbsum/3vhh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3vhh 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).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Biotin-(strept)avidin complex is widely used in biotechnology because of its extremely high binding constant, but there is no report describing spatiotemporally controlled formation of the complex in live cells. Here, based on X-ray crystal structure analysis and calorimetric data, we designed and synthesized photoreleasable biotins, which show greatly reduced affinity for (strept)avidin, but recover native affinity after UV irradiation. For application at the cell surface, we introduced an amine-reactive moiety into these "caged" biotin molecules. Specific fluorescence imaging of live cells that had been labeled with these agents and then UV-irradiated, was accomplished by addition of streptavidin conjugated with a fluorophore. We also demonstrated the applicability of these compounds for UV-irradiated-cell-specific drug delivery by using caged-biotin-labeled cells, a prodrug, and streptavidin conjugated with a prodrug-activating enzyme.


===Crystal structure of DiMe-biotin-avidin complex===
Rational development of caged-biotin protein-labeling agents and some applications in live cells.,Terai T, Maki E, Sugiyama S, Takahashi Y, Matsumura H, Mori Y, Nagano T Chem Biol. 2011 Oct 28;18(10):1261-72. PMID:22035795<ref>PMID:22035795</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3vhh" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_22035795}}, adds the Publication Abstract to the page
*[[Avidin 3D structures|Avidin 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 22035795 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_22035795}}
__TOC__
 
</StructureSection>
==About this Structure==
[[3vhh]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3VHH OCA].
 
==Reference==
<ref group="xtra">PMID:022035795</ref><references group="xtra"/>
[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
[[Category: Maki, E.]]
[[Category: Large Structures]]
[[Category: Matsumura, H.]]
[[Category: Maki E]]
[[Category: Mori, Y.]]
[[Category: Matsumura H]]
[[Category: Nagano, T.]]
[[Category: Mori Y]]
[[Category: Sugiyama, S.]]
[[Category: Nagano T]]
[[Category: Takahashi, Y.]]
[[Category: Sugiyama S]]
[[Category: Terai, T.]]
[[Category: Takahashi Y]]
[[Category: Beta barrel]]
[[Category: Terai T]]
[[Category: Biotin-binding protein]]

Latest revision as of 15:22, 8 November 2023

Crystal structure of DiMe-biotin-avidin complexCrystal structure of DiMe-biotin-avidin complex

Structural highlights

3vhh is a 4 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 2.26Å
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).

Publication Abstract from PubMed

Biotin-(strept)avidin complex is widely used in biotechnology because of its extremely high binding constant, but there is no report describing spatiotemporally controlled formation of the complex in live cells. Here, based on X-ray crystal structure analysis and calorimetric data, we designed and synthesized photoreleasable biotins, which show greatly reduced affinity for (strept)avidin, but recover native affinity after UV irradiation. For application at the cell surface, we introduced an amine-reactive moiety into these "caged" biotin molecules. Specific fluorescence imaging of live cells that had been labeled with these agents and then UV-irradiated, was accomplished by addition of streptavidin conjugated with a fluorophore. We also demonstrated the applicability of these compounds for UV-irradiated-cell-specific drug delivery by using caged-biotin-labeled cells, a prodrug, and streptavidin conjugated with a prodrug-activating enzyme.

Rational development of caged-biotin protein-labeling agents and some applications in live cells.,Terai T, Maki E, Sugiyama S, Takahashi Y, Matsumura H, Mori Y, Nagano T Chem Biol. 2011 Oct 28;18(10):1261-72. PMID:22035795[1]

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

See Also

References

  1. Terai T, Maki E, Sugiyama S, Takahashi Y, Matsumura H, Mori Y, Nagano T. Rational development of caged-biotin protein-labeling agents and some applications in live cells. Chem Biol. 2011 Oct 28;18(10):1261-72. PMID:22035795 doi:10.1016/j.chembiol.2011.09.007

3vhh, resolution 2.26Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA