2qzh

From Proteopedia

(Difference between revisions)

Revision as of 16:59, 10 April 2020

SCR2/3 of DAF from the NMR structure 1nwv fitted into a cryoEM reconstruction of CVB3-RD complexed with DAF

2qzh, resolution 14.00Å

Structural highlights

2qzh is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Experimental data:	Check to display Experimental Data
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[DAF_HUMAN] This protein recognizes C4b and C3b fragments that condense with cell-surface hydroxyl or amino groups when nascent C4b and C3b are locally generated during C4 and c3 activation. Interaction of daf with cell-associated C4b and C3b polypeptides interferes with their ability to catalyze the conversion of C2 and factor B to enzymatically active C2a and Bb and thereby prevents the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade.^[1]

Evolutionary Conservation

Checkto colour the structure by Evolutionary Conservation, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Many entero-, parecho-, and rhinoviruses use immunoglobulin (Ig)-like receptors that bind into the viral canyon and are required to initiate viral uncoating during infection. However, some of these viruses use an alternative or additional receptor that binds outside the canyon. Both the coxsackievirus-adenovirus receptor (CAR), an Ig-like molecule that binds into the viral canyon, and decay-accelerating factor (DAF) have been identified as cellular receptors for coxsackievirus B3 (CVB3). A cryoelectron microscopy reconstruction of a variant of CVB3 complexed with DAF shows full occupancy of the DAF receptor in each of 60 binding sites. The DAF molecule bridges the canyon, blocking the CAR binding site and causing the two receptors to compete with one another. The binding site of DAF on CVB3 differs from the binding site of DAF on the surface of echoviruses, suggesting independent evolutionary processes.

Interaction of decay-accelerating factor with coxsackievirus B3.,Hafenstein S, Bowman VD, Chipman PR, Bator Kelly CM, Lin F, Medof ME, Rossmann MG J Virol. 2007 Dec;81(23):12927-35. Epub 2007 Sep 5. PMID:17804498^[2]

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

References

↑ Ward T, Pipkin PA, Clarkson NA, Stone DM, Minor PD, Almond JW. Decay-accelerating factor CD55 is identified as the receptor for echovirus 7 using CELICS, a rapid immuno-focal cloning method. EMBO J. 1994 Nov 1;13(21):5070-4. PMID:7525274
↑ Hafenstein S, Bowman VD, Chipman PR, Bator Kelly CM, Lin F, Medof ME, Rossmann MG. Interaction of decay-accelerating factor with coxsackievirus B3. J Virol. 2007 Dec;81(23):12927-35. Epub 2007 Sep 5. PMID:17804498 doi:10.1128/JVI.00931-07

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/2qzh"

@@ Line 3: / Line 3: @@
 <SX load='2qzh' size='340' side='right' viewer='molstar' caption='[[2qzh]], [[Resolution|resolution]] 14.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2qzh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QZH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2QZH FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2qzh]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QZH OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2QZH FirstGlance]. <br>
-</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=2qzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qzh OCA], [http://pdbe.org/2qzh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qzh RCSB], [http://www.ebi.ac.uk/pdbsum/2qzh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qzh ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2qzh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qzh OCA], [http://pdbe.org/2qzh PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qzh RCSB], [http://www.ebi.ac.uk/pdbsum/2qzh PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qzh ProSAT]</span></td></tr>
 </table>
 == Function ==

2qzh

From Proteopedia

Revision as of 16:59, 10 April 2020

SCR2/3 of DAF from the NMR structure 1nwv fitted into a cryoEM reconstruction of CVB3-RD complexed with DAF

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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