1yu2
From Proteopedia
(New page: 200px<br /><applet load="1yu2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yu2, resolution 1.86Å" /> '''Major Tropism Determ...) |
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- | [[Image:1yu2.gif|left|200px]]<br /><applet load="1yu2" size=" | + | [[Image:1yu2.gif|left|200px]]<br /><applet load="1yu2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1yu2, resolution 1.86Å" /> | caption="1yu2, resolution 1.86Å" /> | ||
'''Major Tropism Determinant M1 Variant'''<br /> | '''Major Tropism Determinant M1 Variant'''<br /> | ||
==Overview== | ==Overview== | ||
- | Only few instances are known of protein folds that tolerate massive | + | Only few instances are known of protein folds that tolerate massive sequence variation for the sake of binding diversity. The most extensively characterized is the immunoglobulin fold. We now add to this the C-type lectin (CLec) fold, as found in the major tropism determinant (Mtd), a retroelement-encoded receptor-binding protein of Bordetella bacteriophage. Variation in Mtd, with its approximately 10(13) possible sequences, enables phage adaptation to Bordetella spp. Mtd is an intertwined, pyramid-shaped trimer, with variable residues organized by its CLec fold into discrete receptor-binding sites. The CLec fold provides a highly static scaffold for combinatorial display of variable residues, probably reflecting a different evolutionary solution for balancing diversity against stability from that in the immunoglobulin fold. Mtd variants are biased toward the receptor pertactin, and there is evidence that the CLec fold is used broadly for sequence variation by related retroelements. |
==About this Structure== | ==About this Structure== | ||
- | 1YU2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1YU2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YU2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Viruses]] | [[Category: Viruses]] | ||
[[Category: Ghosh, P.]] | [[Category: Ghosh, P.]] | ||
- | [[Category: Lawton, J | + | [[Category: Lawton, J A.]] |
- | [[Category: McMahon, S | + | [[Category: McMahon, S A.]] |
- | [[Category: Miller, J | + | [[Category: Miller, J L.]] |
[[Category: MG]] | [[Category: MG]] | ||
[[Category: beta prism]] | [[Category: beta prism]] | ||
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[[Category: variability]] | [[Category: variability]] | ||
- | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:07 2008'' |
Revision as of 14:09, 21 February 2008
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Major Tropism Determinant M1 Variant
Overview
Only few instances are known of protein folds that tolerate massive sequence variation for the sake of binding diversity. The most extensively characterized is the immunoglobulin fold. We now add to this the C-type lectin (CLec) fold, as found in the major tropism determinant (Mtd), a retroelement-encoded receptor-binding protein of Bordetella bacteriophage. Variation in Mtd, with its approximately 10(13) possible sequences, enables phage adaptation to Bordetella spp. Mtd is an intertwined, pyramid-shaped trimer, with variable residues organized by its CLec fold into discrete receptor-binding sites. The CLec fold provides a highly static scaffold for combinatorial display of variable residues, probably reflecting a different evolutionary solution for balancing diversity against stability from that in the immunoglobulin fold. Mtd variants are biased toward the receptor pertactin, and there is evidence that the CLec fold is used broadly for sequence variation by related retroelements.
About this Structure
1YU2 is a Single protein structure of sequence from Viruses with as ligand. Full crystallographic information is available from OCA.
Reference
The C-type lectin fold as an evolutionary solution for massive sequence variation., McMahon SA, Miller JL, Lawton JA, Kerkow DE, Hodes A, Marti-Renom MA, Doulatov S, Narayanan E, Sali A, Miller JF, Ghosh P, Nat Struct Mol Biol. 2005 Oct;12(10):886-92. Epub 2005 Sep 18. PMID:16170324
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