1xph
From Proteopedia
(New page: 200px<br /> <applet load="1xph" size="450" color="white" frame="true" align="right" spinBox="true" caption="1xph, resolution 1.41Å" /> '''Structure of DC-SIG...) |
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| - | [[Image:1xph.gif|left|200px]]<br /> | + | [[Image:1xph.gif|left|200px]]<br /><applet load="1xph" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1xph" size=" | + | |
caption="1xph, resolution 1.41Å" /> | caption="1xph, resolution 1.41Å" /> | ||
'''Structure of DC-SIGNR and a portion of repeat domain 8'''<br /> | '''Structure of DC-SIGNR and a portion of repeat domain 8'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The dendritic cell-specific ICAM-3 non-integrin (DC-SIGN) and its close | + | The dendritic cell-specific ICAM-3 non-integrin (DC-SIGN) and its close relative DC-SIGNR recognize various glycoproteins, both pathogenic and cellular, through the receptor lectin domain-mediated carbohydrate recognition. While the carbohydrate-recognition domains (CRD) exist as monomers and bind individual carbohydrates with low affinity and are permissive in nature, the full-length receptors form tetramers through their repeat domain and recognize specific ligands with high affinity. To understand the tetramer-based ligand binding avidity, we determined the crystal structure of DC-SIGNR with its last repeat region. Compared to the carbohydrate-bound CRD structure, the structure revealed conformational changes in the calcium and carbohydrate coordination loops of CRD, an additional disulfide bond between the N and the C termini of the CRD, and a helical conformation for the last repeat. On the basis of the current crystal structure and other published structures with sequence homology to the repeat domain, we generated a tetramer model for DC-SIGN/R using homology modeling and propose a ligand-recognition index to identify potential receptor ligands. |
==Disease== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1XPH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1XPH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1XPH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Colonna, M.]] | [[Category: Colonna, M.]] | ||
| - | [[Category: Snyder, G | + | [[Category: Snyder, G A.]] |
| - | [[Category: Sun, P | + | [[Category: Sun, P D.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: c-type lectin]] | [[Category: c-type lectin]] | ||
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[[Category: repeat domain]] | [[Category: repeat domain]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:57:14 2008'' |
Revision as of 13:57, 21 February 2008
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Structure of DC-SIGNR and a portion of repeat domain 8
Contents |
Overview
The dendritic cell-specific ICAM-3 non-integrin (DC-SIGN) and its close relative DC-SIGNR recognize various glycoproteins, both pathogenic and cellular, through the receptor lectin domain-mediated carbohydrate recognition. While the carbohydrate-recognition domains (CRD) exist as monomers and bind individual carbohydrates with low affinity and are permissive in nature, the full-length receptors form tetramers through their repeat domain and recognize specific ligands with high affinity. To understand the tetramer-based ligand binding avidity, we determined the crystal structure of DC-SIGNR with its last repeat region. Compared to the carbohydrate-bound CRD structure, the structure revealed conformational changes in the calcium and carbohydrate coordination loops of CRD, an additional disulfide bond between the N and the C termini of the CRD, and a helical conformation for the last repeat. On the basis of the current crystal structure and other published structures with sequence homology to the repeat domain, we generated a tetramer model for DC-SIGN/R using homology modeling and propose a ligand-recognition index to identify potential receptor ligands.
Disease
Known disease associated with this structure: SARS infection, protection against OMIM:[605872]
About this Structure
1XPH is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
The structure of DC-SIGNR with a portion of its repeat domain lends insights to modeling of the receptor tetramer., Snyder GA, Colonna M, Sun PD, J Mol Biol. 2005 Apr 15;347(5):979-89. PMID:15784257
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