1ijs
From Proteopedia
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| - | [[Image:1ijs.gif|left|200px]] | + | [[Image:1ijs.gif|left|200px]] |
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| - | '''CPV(STRAIN D) MUTANT A300D, COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C''' | + | {{Structure |
| + | |PDB= 1ijs |SIZE=350|CAPTION= <scene name='initialview01'>1ijs</scene>, resolution 3.250Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''CPV(STRAIN D) MUTANT A300D, COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1IJS is a [ | + | 1IJS is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Canine_parvovirus Canine parvovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IJS OCA]. |
==Reference== | ==Reference== | ||
| - | Structural analysis of a mutation in canine parvovirus which controls antigenicity and host range., Llamas-Saiz AL, Agbandje-McKenna M, Parker JS, Wahid AT, Parrish CR, Rossmann MG, Virology. 1996 Nov 1;225(1):65-71. PMID:[http:// | + | Structural analysis of a mutation in canine parvovirus which controls antigenicity and host range., Llamas-Saiz AL, Agbandje-McKenna M, Parker JS, Wahid AT, Parrish CR, Rossmann MG, Virology. 1996 Nov 1;225(1):65-71. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8918534 8918534] |
[[Category: Canine parvovirus]] | [[Category: Canine parvovirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: viral coat protein]] | [[Category: viral coat protein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:51:15 2008'' |
Revision as of 09:51, 20 March 2008
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| , resolution 3.250Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CPV(STRAIN D) MUTANT A300D, COMPLEX(VIRAL COAT/DNA), VP2, PH=7.5, T=4 DEGREES C
Overview
A single mutation in canine parvovirus (CPV) of VP2 residue 300 from alanine to aspartic acid causes a loss of canine host range and alters the antigenic properties of the virus. The three-dimensional structure of this mutant has been solved to 3.25 A resolution. Crystals of full particles were triclinic, with cell dimensions of a = 267.6, b = 268.5, c = 274.3 A. alpha = 61.9, beta = 62.6, and gamma = 60.2 degrees. The native structure of CPV was used as an initial model. Phases were improved by real-space electron density averaging. In spite of the relative low percentage of observed reflections (32.5% of the data between 15.0 and 3.25 A resolution), the presence of 60-fold noncrystallographic redundancy allowed the averaging procedure to converge smoothly. The mutant aspartic acid at residue 300 forms a salt bridge with Arg81 in an icosahedrally threefold-related subunit, inducing local changes within the antigenic site B on the CPV surface. In addition, the loop between residues 359 and 374 adopts a conformation similar to that displayed by feline panleukopenia virus. The ability of the Ala300-->Asp mutant to evade antibody binding can be associated with the change of charge distribution and structure in the antigenic binding site. The variation in host range behavior may be due to the increased stability as a result of formation of the salt bridge between adjacent subunits.
About this Structure
1IJS is a Single protein structure of sequence from Canine parvovirus. Full crystallographic information is available from OCA.
Reference
Structural analysis of a mutation in canine parvovirus which controls antigenicity and host range., Llamas-Saiz AL, Agbandje-McKenna M, Parker JS, Wahid AT, Parrish CR, Rossmann MG, Virology. 1996 Nov 1;225(1):65-71. PMID:8918534
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