1avp
From Proteopedia
(New page: 200px<br /><applet load="1avp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1avp, resolution 2.6Å" /> '''STRUCTURE OF HUMAN AD...) |
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| - | [[Image:1avp.gif|left|200px]]<br /><applet load="1avp" size=" | + | [[Image:1avp.gif|left|200px]]<br /><applet load="1avp" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1avp, resolution 2.6Å" /> | caption="1avp, resolution 2.6Å" /> | ||
'''STRUCTURE OF HUMAN ADENOVIRUS 2 PROTEINASE WITH ITS 11 AMINO ACID COFACTOR'''<br /> | '''STRUCTURE OF HUMAN ADENOVIRUS 2 PROTEINASE WITH ITS 11 AMINO ACID COFACTOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the human adenovirus-2 proteinase | + | The three-dimensional structure of the human adenovirus-2 proteinase complexed with its 11 amino acid cofactor, pVIc, was determined at 2.6 A resolution by X-ray crystallographic analysis. The fold of this protein has not been seen before. However, it represents an example of either subtly divergent or powerfully convergent evolution, because the active site contains a Cys-His-Glu triplet and oxyanion hole in an arrangement similar to that in papain. Thus, the adenovirus proteinase represents a new, fifth group of enzymes that contain catalytic triads. pVIc, which extends a beta-sheet in the main chain, is distant from the active site, yet its binding increases the catalytic rate constant 300-fold for substrate hydrolysis. The structure reveals several potential targets for antiviral therapy. |
==About this Structure== | ==About this Structure== | ||
| - | 1AVP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_adenovirus_2 Human adenovirus 2]. Full crystallographic information is available from [http:// | + | 1AVP is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_adenovirus_2 Human adenovirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AVP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein complex]] | [[Category: Protein complex]] | ||
[[Category: Ding, J.]] | [[Category: Ding, J.]] | ||
| - | [[Category: Mangel, W | + | [[Category: Mangel, W F.]] |
| - | [[Category: Mcgrath, W | + | [[Category: Mcgrath, W J.]] |
| - | [[Category: Sweet, R | + | [[Category: Sweet, R M.]] |
[[Category: peptide cofactor]] | [[Category: peptide cofactor]] | ||
[[Category: thiol hydrolase]] | [[Category: thiol hydrolase]] | ||
[[Category: viral proteinase]] | [[Category: viral proteinase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:48:45 2008'' |
Revision as of 09:48, 21 February 2008
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STRUCTURE OF HUMAN ADENOVIRUS 2 PROTEINASE WITH ITS 11 AMINO ACID COFACTOR
Overview
The three-dimensional structure of the human adenovirus-2 proteinase complexed with its 11 amino acid cofactor, pVIc, was determined at 2.6 A resolution by X-ray crystallographic analysis. The fold of this protein has not been seen before. However, it represents an example of either subtly divergent or powerfully convergent evolution, because the active site contains a Cys-His-Glu triplet and oxyanion hole in an arrangement similar to that in papain. Thus, the adenovirus proteinase represents a new, fifth group of enzymes that contain catalytic triads. pVIc, which extends a beta-sheet in the main chain, is distant from the active site, yet its binding increases the catalytic rate constant 300-fold for substrate hydrolysis. The structure reveals several potential targets for antiviral therapy.
About this Structure
1AVP is a Protein complex structure of sequences from Human adenovirus 2. Full crystallographic information is available from OCA.
Reference
Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor., Ding J, McGrath WJ, Sweet RM, Mangel WF, EMBO J. 1996 Apr 15;15(8):1778-83. PMID:8617222
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