1r1a
From Proteopedia
(New page: 200px<br /><applet load="1r1a" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r1a, resolution 3.2Å" /> '''CRYSTAL STRUCTURE OF ...) |
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| - | [[Image:1r1a.jpg|left|200px]]<br /><applet load="1r1a" size=" | + | [[Image:1r1a.jpg|left|200px]]<br /><applet load="1r1a" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1r1a, resolution 3.2Å" /> | caption="1r1a, resolution 3.2Å" /> | ||
'''CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS SEROTYPE 1A (HRV1A)'''<br /> | '''CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS SEROTYPE 1A (HRV1A)'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 A | + | The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 A resolution using phase refinement and extension by symmetry averaging starting with phases at 5 A resolution calculated from the known human rhinovirus 14 (HRV14) structure. The polypeptide backbone structures of HRV1A and HRV14 are similar, but the exposed surfaces are rather different. Differential charge distribution of amino acid residues in the "canyon", the putative receptor binding site, provides a possible explanation for the difference in minor versus major receptor group specificities, represented by HRV1A and HRV14, respectively. The hydrophobic pocket in VP1, into which antiviral compounds bind, is in an "open" conformation similar to that observed in drug-bound HRV14. Drug binding in HRV1A does not induce extensive conformational changes, in contrast to the case of HRV14. |
==About this Structure== | ==About this Structure== | ||
| - | 1R1A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_rhinovirus_a Human rhinovirus a] with SUC as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1R1A is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_rhinovirus_a Human rhinovirus a] with <scene name='pdbligand=SUC:'>SUC</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R1A OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Kim, S.]] | [[Category: Kim, S.]] | ||
| - | [[Category: Rossmann, M | + | [[Category: Rossmann, M G.]] |
[[Category: SUC]] | [[Category: SUC]] | ||
[[Category: icosahedral virus]] | [[Category: icosahedral virus]] | ||
[[Category: rhinovirus coat protein]] | [[Category: rhinovirus coat protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:46:01 2008'' |
Revision as of 12:46, 21 February 2008
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CRYSTAL STRUCTURE OF HUMAN RHINOVIRUS SEROTYPE 1A (HRV1A)
Overview
The structure of human rhinovirus 1A (HRV1A) has been determined to 3.2 A resolution using phase refinement and extension by symmetry averaging starting with phases at 5 A resolution calculated from the known human rhinovirus 14 (HRV14) structure. The polypeptide backbone structures of HRV1A and HRV14 are similar, but the exposed surfaces are rather different. Differential charge distribution of amino acid residues in the "canyon", the putative receptor binding site, provides a possible explanation for the difference in minor versus major receptor group specificities, represented by HRV1A and HRV14, respectively. The hydrophobic pocket in VP1, into which antiviral compounds bind, is in an "open" conformation similar to that observed in drug-bound HRV14. Drug binding in HRV1A does not induce extensive conformational changes, in contrast to the case of HRV14.
About this Structure
1R1A is a Protein complex structure of sequences from Human rhinovirus a with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal structure of human rhinovirus serotype 1A (HRV1A)., Kim SS, Smith TJ, Chapman MS, Rossmann MC, Pevear DC, Dutko FJ, Felock PJ, Diana GD, McKinlay MA, J Mol Biol. 1989 Nov 5;210(1):91-111. PMID:2555523
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