1jrf
From Proteopedia
(New page: 200px<br /><applet load="1jrf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jrf" /> '''NMR Solution Structure of the Viral Receptor...) |
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| - | [[Image:1jrf.jpg|left|200px]]<br /><applet load="1jrf" size=" | + | [[Image:1jrf.jpg|left|200px]]<br /><applet load="1jrf" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jrf" /> | caption="1jrf" /> | ||
'''NMR Solution Structure of the Viral Receptor Domain of Tva'''<br /> | '''NMR Solution Structure of the Viral Receptor Domain of Tva'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tva is the cellular receptor for subgroup A avian sarcoma and leukosis | + | Tva is the cellular receptor for subgroup A avian sarcoma and leukosis virus (ASLV-A). The viral receptor function of Tva is determined by a 40-residue, cysteine-rich motif called the LDL-A module. Here we report the solution structure of the LDL-A module of Tva, determined by nuclear magnetic resonance (NMR) spectroscopy. Although the carboxyl terminus of the Tva LDL-A module has a structure similar to those of other reported LDL-A modules, the amino terminus adopts a different conformation. The LDL-A module of Tva does not contain the signature antiparallel beta-sheet observed in other LDL-A modules, and it is more flexible than other reported LDL-A modules. The LDL-A structure of Tva provides mechanistic insights into how a simple viral receptor functions in retrovirus entry. The side chains of H38 and W48 of Tva, which have been identified as viral contact residues by mutational analysis, are solvent exposed, suggesting that they are directly involved in EnvA binding. However, the side chain of L34, another potential viral contact residue identified previously, is buried inside of the module and forms the hydrophobic core with other residues. Thus L34 likely stabilizes the Tva structure but is not a viral interaction determinant. In addition, we propose that the flexible amino-terminal region of Tva plays an important role in determining specificity in the Tva-EnvA interaction. |
==About this Structure== | ==About this Structure== | ||
| - | 1JRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Coturnix_japonica Coturnix japonica] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1JRF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Coturnix_japonica Coturnix japonica] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JRF OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Dolmer, K.]] | [[Category: Dolmer, K.]] | ||
| - | [[Category: Gettins, P | + | [[Category: Gettins, P G.W.]] |
[[Category: Huang, W.]] | [[Category: Huang, W.]] | ||
[[Category: Rong, L.]] | [[Category: Rong, L.]] | ||
| - | [[Category: Wang, Q | + | [[Category: Wang, Q Y.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: alpha helix]] | [[Category: alpha helix]] | ||
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[[Category: disulfide bond]] | [[Category: disulfide bond]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:03 2008'' |
Revision as of 11:26, 21 February 2008
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NMR Solution Structure of the Viral Receptor Domain of Tva
Overview
Tva is the cellular receptor for subgroup A avian sarcoma and leukosis virus (ASLV-A). The viral receptor function of Tva is determined by a 40-residue, cysteine-rich motif called the LDL-A module. Here we report the solution structure of the LDL-A module of Tva, determined by nuclear magnetic resonance (NMR) spectroscopy. Although the carboxyl terminus of the Tva LDL-A module has a structure similar to those of other reported LDL-A modules, the amino terminus adopts a different conformation. The LDL-A module of Tva does not contain the signature antiparallel beta-sheet observed in other LDL-A modules, and it is more flexible than other reported LDL-A modules. The LDL-A structure of Tva provides mechanistic insights into how a simple viral receptor functions in retrovirus entry. The side chains of H38 and W48 of Tva, which have been identified as viral contact residues by mutational analysis, are solvent exposed, suggesting that they are directly involved in EnvA binding. However, the side chain of L34, another potential viral contact residue identified previously, is buried inside of the module and forms the hydrophobic core with other residues. Thus L34 likely stabilizes the Tva structure but is not a viral interaction determinant. In addition, we propose that the flexible amino-terminal region of Tva plays an important role in determining specificity in the Tva-EnvA interaction.
About this Structure
1JRF is a Single protein structure of sequence from Coturnix japonica with as ligand. Full crystallographic information is available from OCA.
Reference
Solution structure of the viral receptor domain of Tva and its implications in viral entry., Wang QY, Huang W, Dolmer K, Gettins PG, Rong L, J Virol. 2002 Mar;76(6):2848-56. PMID:11861852
Page seeded by OCA on Thu Feb 21 13:26:03 2008
