1xph: Difference between revisions

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New page: left|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="450" color="white" frame="true" align="right" spinBox="true"  
caption="1xph, resolution 1.41&Aring;" />
caption="1xph, resolution 1.41&Aring;" />
'''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, 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.
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1XPH OCA].  
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.A.]]
[[Category: Snyder, G A.]]
[[Category: Sun, P.D.]]
[[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://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:09:19 2007''
''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

File:1xph.gif


1xph, resolution 1.41Å

Drag the structure with the mouse to rotate

Structure of DC-SIGNR and a portion of repeat domain 8

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 CA 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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