2or8

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(New page: 200px<br /><applet load="2or8" size="450" color="white" frame="true" align="right" spinBox="true" caption="2or8, resolution 2.5&Aring;" /> '''Tim-1'''<br /> ==Ove...)
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[[Image:2or8.gif|left|200px]]<br /><applet load="2or8" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:2or8.gif|left|200px]]<br /><applet load="2or8" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2or8, resolution 2.5&Aring;" />
caption="2or8, resolution 2.5&Aring;" />
'''Tim-1'''<br />
'''Tim-1'''<br />
==Overview==
==Overview==
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The T cell immunoglobulin mucin (TIM) receptors are involved in the, regulation of immune responses, autoimmunity, and allergy. Structures of, the N-terminal ligand binding domain of the murine mTIM-1 and mTIM-2, receptors revealed an immunoglobulin (Ig) fold, with four Cys residues, bridging a distinctive CC' loop to the GFC beta-sheet. The structures, showed two ligand-recognition modes in the TIM family. The mTIM-1, structure identified a homophilic TIM-TIM adhesion interaction, whereas, the mTIM-2 domain formed a dimer that prevented homophilic binding., Biochemical, mutational, and cell adhesion analyses confirmed the, divergent ligand-binding modes revealed by the structures. Structural, features characteristic of mTIM-1 appear conserved in human TIM-1, which, also mediated homophilic interactions. The extracellular mucin domain, enhanced binding through the Ig domain, modulating TIM receptor functions., These results explain the divergent immune functions described for the, murine receptors and the role of TIM-1 as a cell adhesion receptor in, renal regeneration and cancer.
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The T cell immunoglobulin mucin (TIM) receptors are involved in the regulation of immune responses, autoimmunity, and allergy. Structures of the N-terminal ligand binding domain of the murine mTIM-1 and mTIM-2 receptors revealed an immunoglobulin (Ig) fold, with four Cys residues bridging a distinctive CC' loop to the GFC beta-sheet. The structures showed two ligand-recognition modes in the TIM family. The mTIM-1 structure identified a homophilic TIM-TIM adhesion interaction, whereas the mTIM-2 domain formed a dimer that prevented homophilic binding. Biochemical, mutational, and cell adhesion analyses confirmed the divergent ligand-binding modes revealed by the structures. Structural features characteristic of mTIM-1 appear conserved in human TIM-1, which also mediated homophilic interactions. The extracellular mucin domain enhanced binding through the Ig domain, modulating TIM receptor functions. These results explain the divergent immune functions described for the murine receptors and the role of TIM-1 as a cell adhesion receptor in renal regeneration and cancer.
==About this Structure==
==About this Structure==
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2OR8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with ACT as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OR8 OCA].
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2OR8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=ACT:'>ACT</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2OR8 OCA].
==Reference==
==Reference==
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Structures of T Cell Immunoglobulin Mucin Receptors 1 and 2 Reveal Mechanisms for Regulation of Immune Responses by the TIM Receptor Family., Santiago C, Ballesteros A, Tami C, Martinez-Munoz L, Kaplan GG, Casasnovas JM, Immunity. 2007 Mar;26(3):299-310. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17363299 17363299]
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Structures of T Cell immunoglobulin mucin receptors 1 and 2 reveal mechanisms for regulation of immune responses by the TIM receptor family., Santiago C, Ballesteros A, Tami C, Martinez-Munoz L, Kaplan GG, Casasnovas JM, Immunity. 2007 Mar;26(3):299-310. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17363299 17363299]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ballesteros, A.]]
[[Category: Ballesteros, A.]]
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[[Category: Casasnovas, J.M.]]
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[[Category: Casasnovas, J M.]]
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[[Category: Kaplan, G.G.]]
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[[Category: Kaplan, G G.]]
[[Category: Santiago, C.]]
[[Category: Santiago, C.]]
[[Category: ACT]]
[[Category: ACT]]
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[[Category: tim]]
[[Category: tim]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:16:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:21:39 2008''

Revision as of 16:21, 21 February 2008


2or8, resolution 2.5Å

Drag the structure with the mouse to rotate

Tim-1

Overview

The T cell immunoglobulin mucin (TIM) receptors are involved in the regulation of immune responses, autoimmunity, and allergy. Structures of the N-terminal ligand binding domain of the murine mTIM-1 and mTIM-2 receptors revealed an immunoglobulin (Ig) fold, with four Cys residues bridging a distinctive CC' loop to the GFC beta-sheet. The structures showed two ligand-recognition modes in the TIM family. The mTIM-1 structure identified a homophilic TIM-TIM adhesion interaction, whereas the mTIM-2 domain formed a dimer that prevented homophilic binding. Biochemical, mutational, and cell adhesion analyses confirmed the divergent ligand-binding modes revealed by the structures. Structural features characteristic of mTIM-1 appear conserved in human TIM-1, which also mediated homophilic interactions. The extracellular mucin domain enhanced binding through the Ig domain, modulating TIM receptor functions. These results explain the divergent immune functions described for the murine receptors and the role of TIM-1 as a cell adhesion receptor in renal regeneration and cancer.

About this Structure

2OR8 is a Single protein structure of sequence from Mus musculus with as ligand. Full crystallographic information is available from OCA.

Reference

Structures of T Cell immunoglobulin mucin receptors 1 and 2 reveal mechanisms for regulation of immune responses by the TIM receptor family., Santiago C, Ballesteros A, Tami C, Martinez-Munoz L, Kaplan GG, Casasnovas JM, Immunity. 2007 Mar;26(3):299-310. PMID:17363299

Page seeded by OCA on Thu Feb 21 18:21:39 2008

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