1z6i

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(New page: 200px<br /><applet load="1z6i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1z6i, resolution 2.50&Aring;" /> '''Crystal structure of...)
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[[Image:1z6i.gif|left|200px]]<br /><applet load="1z6i" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1z6i, resolution 2.50&Aring;" />
caption="1z6i, resolution 2.50&Aring;" />
'''Crystal structure of the ectodomain of Drosophila transmembrane receptor PGRP-LCa'''<br />
'''Crystal structure of the ectodomain of Drosophila transmembrane receptor PGRP-LCa'''<br />
==Overview==
==Overview==
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The peptidoglycan-recognition protein LCa (PGRP-LCa) is a transmembrane, receptor required for activation of the Drosophila immune deficiency, pathway by monomeric Gram-negative peptidoglycan. We have determined the, crystal structure of the ectodomain of PGRP-LCa at 2.5-A resolution and, found two unique helical insertions in the LCa ectodomain that disrupt an, otherwise L-shaped peptidoglycan-docking groove present in all other known, PGRP structures. The deficient binding of PGRP-LCa to monomeric, peptidoglycan was confirmed by biochemical pull-down assays. Recognition, of monomeric peptidoglycan involves both PGRP-LCa and -LCx. We showed that, association of the LCa and LCx ectodomains in vitro depends on monomeric, peptidoglycan. The presence of a defective peptidoglycan-docking groove, while preserving a unique role in mediating monomeric peptidoglycan, induction of immune response, suggests that PGRP-LCa recognizes the, exposed structural features of a monomeric muropeptide when the latter is, bound to and presented by the ectodomain of PGRP-LCx. Such features, include N-acetyl glucosamine and the anhydro bond in the glycan of the, muropeptide, which have been demonstrated to be critical for immune, stimulatory activity.
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The peptidoglycan-recognition protein LCa (PGRP-LCa) is a transmembrane receptor required for activation of the Drosophila immune deficiency pathway by monomeric Gram-negative peptidoglycan. We have determined the crystal structure of the ectodomain of PGRP-LCa at 2.5-A resolution and found two unique helical insertions in the LCa ectodomain that disrupt an otherwise L-shaped peptidoglycan-docking groove present in all other known PGRP structures. The deficient binding of PGRP-LCa to monomeric peptidoglycan was confirmed by biochemical pull-down assays. Recognition of monomeric peptidoglycan involves both PGRP-LCa and -LCx. We showed that association of the LCa and LCx ectodomains in vitro depends on monomeric peptidoglycan. The presence of a defective peptidoglycan-docking groove, while preserving a unique role in mediating monomeric peptidoglycan induction of immune response, suggests that PGRP-LCa recognizes the exposed structural features of a monomeric muropeptide when the latter is bound to and presented by the ectodomain of PGRP-LCx. Such features include N-acetyl glucosamine and the anhydro bond in the glycan of the muropeptide, which have been demonstrated to be critical for immune stimulatory activity.
==About this Structure==
==About this Structure==
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1Z6I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with NAG and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Z6I OCA].
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1Z6I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with <scene name='pdbligand=NAG:'>NAG</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Z6I OCA].
==Reference==
==Reference==
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Chang, C.I.]]
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[[Category: Chang, C I.]]
[[Category: Chelliah, Y.]]
[[Category: Chelliah, Y.]]
[[Category: Deisenhofer, J.]]
[[Category: Deisenhofer, J.]]
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[[Category: mixed beta-sheet]]
[[Category: mixed beta-sheet]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 07:15:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:12:32 2008''

Revision as of 14:12, 21 February 2008


1z6i, resolution 2.50Å

Drag the structure with the mouse to rotate

Crystal structure of the ectodomain of Drosophila transmembrane receptor PGRP-LCa

Overview

The peptidoglycan-recognition protein LCa (PGRP-LCa) is a transmembrane receptor required for activation of the Drosophila immune deficiency pathway by monomeric Gram-negative peptidoglycan. We have determined the crystal structure of the ectodomain of PGRP-LCa at 2.5-A resolution and found two unique helical insertions in the LCa ectodomain that disrupt an otherwise L-shaped peptidoglycan-docking groove present in all other known PGRP structures. The deficient binding of PGRP-LCa to monomeric peptidoglycan was confirmed by biochemical pull-down assays. Recognition of monomeric peptidoglycan involves both PGRP-LCa and -LCx. We showed that association of the LCa and LCx ectodomains in vitro depends on monomeric peptidoglycan. The presence of a defective peptidoglycan-docking groove, while preserving a unique role in mediating monomeric peptidoglycan induction of immune response, suggests that PGRP-LCa recognizes the exposed structural features of a monomeric muropeptide when the latter is bound to and presented by the ectodomain of PGRP-LCx. Such features include N-acetyl glucosamine and the anhydro bond in the glycan of the muropeptide, which have been demonstrated to be critical for immune stimulatory activity.

About this Structure

1Z6I is a Single protein structure of sequence from Drosophila melanogaster with and as ligands. Full crystallographic information is available from OCA.

Reference

Structure of the ectodomain of Drosophila peptidoglycan-recognition protein LCa suggests a molecular mechanism for pattern recognition., Chang CI, Ihara K, Chelliah Y, Mengin-Lecreulx D, Wakatsuki S, Deisenhofer J, Proc Natl Acad Sci U S A. 2005 Jul 19;102(29):10279-84. Epub 2005 Jul 8. PMID:16006509

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