2j1k
From Proteopedia
(Difference between revisions)
| Line 2: | Line 2: | ||
<StructureSection load='2j1k' size='340' side='right' caption='[[2j1k]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='2j1k' size='340' side='right' caption='[[2j1k]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | [[2j1k]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Canine_adenovirus_2 Canine adenovirus 2] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J1K OCA]. <br> | + | <table><tr><td colspan='2'>[[2j1k]] is a 24 chain structure with sequence from [http://en.wikipedia.org/wiki/Canine_adenovirus_2 Canine adenovirus 2] and [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J1K OCA]. <br> |
| - | <b>[[Related_structure|Related:]]</b> [[1kac|1kac]], [[1nob|1nob]], [[1p69|1p69]], [[1p6a|1p6a]]< | + | </td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1kac|1kac]], [[1nob|1nob]], [[1p69|1p69]], [[1p6a|1p6a]]</td></tr> |
| - | <b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span>< | + | <tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span></td></tr> |
| - | <b>Resources:</b> <span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j1k RCSB], [http://www.ebi.ac.uk/pdbsum/2j1k PDBsum]</span>< | + | <tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j1k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j1k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2j1k RCSB], [http://www.ebi.ac.uk/pdbsum/2j1k PDBsum]</span></td></tr> |
| + | <table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
| - | [[Image:Consurf_key_small.gif|right]] | + | [[Image:Consurf_key_small.gif|200px|right]] |
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
| Line 16: | Line 17: | ||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
Adenovirus fibers from most serotypes bind the D1 domain of coxsackie and adenovirus receptor (CAR), although the binding residues are not strictly conserved. To understand this further, we determined the crystal structures of canine adenovirus serotype 2 (CAV-2) and the human adenovirus serotype 37 (HAd37) in complex with human CAR D1 at 2.3 and 1.5A resolution, respectively. Structure comparison with the HAd12 fiber head-CAR D1 complex showed that the overall topology of the interaction is conserved but that the interfaces differ in number and identity of interacting residues, shape complementarity, and degree of conformational adaptation. Using surface plasmon resonance, we characterized the binding affinity to CAR D1 of wild type and mutant CAV-2 and HAd37 fiber heads. We found that CAV-2 has the highest affinity but fewest direct interactions, with the reverse being true for HAd37. Moreover, we found that conserved interactions can have a minor contribution, whereas serotype-specific interactions can be essential. These results are discussed in the light of virus evolution and design of adenovirus vectors for gene transfer. | Adenovirus fibers from most serotypes bind the D1 domain of coxsackie and adenovirus receptor (CAR), although the binding residues are not strictly conserved. To understand this further, we determined the crystal structures of canine adenovirus serotype 2 (CAV-2) and the human adenovirus serotype 37 (HAd37) in complex with human CAR D1 at 2.3 and 1.5A resolution, respectively. Structure comparison with the HAd12 fiber head-CAR D1 complex showed that the overall topology of the interaction is conserved but that the interfaces differ in number and identity of interacting residues, shape complementarity, and degree of conformational adaptation. Using surface plasmon resonance, we characterized the binding affinity to CAR D1 of wild type and mutant CAV-2 and HAd37 fiber heads. We found that CAV-2 has the highest affinity but fewest direct interactions, with the reverse being true for HAd37. Moreover, we found that conserved interactions can have a minor contribution, whereas serotype-specific interactions can be essential. These results are discussed in the light of virus evolution and design of adenovirus vectors for gene transfer. | ||
| Line 22: | Line 24: | ||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 09:52, 1 May 2014
CAV-2 FIBRE HEAD IN COMPLEX WITH CAR D1
| |||||||||||
Categories: Canine adenovirus 2 | Homo sapiens | Billet, O. | Cusack, S. | Kremer, E J. | Lortat-Jacob, H. | Seiradake, E. | Adenovirus | Canine | Car | Cav-2 | Cell adhesion | Complex | Coxsackievirus | Domain d1 | Fiber | Fiber head | Fiber protein | Fibre | Fibre head | Glycoprotein | Host-virus interaction | Immunoglobulin domain | Knob | Lipoprotein | Membrane | Palmitate | Phosphorylation | Receptor | Tight junction | Transmembrane | Virus-receptor complex
