2j12
From Proteopedia
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|PDB= 2j12 |SIZE=350|CAPTION= <scene name='initialview01'>2j12</scene>, resolution 1.50Å | |PDB= 2j12 |SIZE=350|CAPTION= <scene name='initialview01'>2j12</scene>, resolution 1.50Å | ||
|SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Ca+Binding+Site+For+Chain+B'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2j12 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j12 OCA], [http://www.ebi.ac.uk/pdbsum/2j12 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2j12 RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Adrenocortical tumor, somatic OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]], Carney complex, type 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]], Myxoma, intracardiac OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]], Pigmented adrenocortical disease, primary, 1 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]], Spastic paraplegia-7 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=602783 602783]], Thyroid carcinoma, papillary OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=188830 188830]] | ||
==About this Structure== | ==About this Structure== | ||
| - | 2J12 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/ | + | 2J12 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [http://en.wikipedia.org/wiki/Human_adenovirus_37 Human adenovirus 37]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J12 OCA]. |
==Reference== | ==Reference== | ||
Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor., Seiradake E, Lortat-Jacob H, Billet O, Kremer EJ, Cusack S, J Biol Chem. 2006 Nov 3;281(44):33704-16. Epub 2006 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16923808 16923808] | Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor., Seiradake E, Lortat-Jacob H, Billet O, Kremer EJ, Cusack S, J Biol Chem. 2006 Nov 3;281(44):33704-16. Epub 2006 Aug 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16923808 16923808] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
| - | [[Category: Human adenovirus | + | [[Category: Human adenovirus 37]] |
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Billet, O.]] | [[Category: Billet, O.]] | ||
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[[Category: Lortat-Jacob, H.]] | [[Category: Lortat-Jacob, H.]] | ||
[[Category: Seiradake, E.]] | [[Category: Seiradake, E.]] | ||
| - | [[Category: CA]] | ||
[[Category: ad37]] | [[Category: ad37]] | ||
[[Category: adenovirus]] | [[Category: adenovirus]] | ||
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[[Category: x-ray]] | [[Category: x-ray]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:51:34 2008'' |
Revision as of 00:51, 31 March 2008
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| , resolution 1.50Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
AD37 FIBRE HEAD IN COMPLEX WITH CAR D1
Overview
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.
About this Structure
2J12 is a Protein complex structure of sequences from Homo sapiens and Human adenovirus 37. Full crystallographic information is available from OCA.
Reference
Structural and mutational analysis of human Ad37 and canine adenovirus 2 fiber heads in complex with the D1 domain of coxsackie and adenovirus receptor., Seiradake E, Lortat-Jacob H, Billet O, Kremer EJ, Cusack S, J Biol Chem. 2006 Nov 3;281(44):33704-16. Epub 2006 Aug 21. PMID:16923808
Page seeded by OCA on Mon Mar 31 03:51:34 2008
Categories: Homo sapiens | Human adenovirus 37 | Protein complex | Billet, O. | Cusac, S. | Kremer, E J. | Lortat-Jacob, H. | Seiradake, E. | Ad37 | Adenovirus | Alternative splicing | Car | Cell adhesion | Complex | Coxsackievirus | Glycoprotein | Had37 | Host-virus interaction | Immunoglobulin domain | Lipoprotein | Membrane | Palmitate | Phosphorylation | Receptor | Tight junction | Transmembrane | Viral protein/receptor complex | X-ray
