1nt0

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(New page: 200px<br /><applet load="1nt0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1nt0, resolution 2.70&Aring;" /> '''Crystal structure of...)
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[[Image:1nt0.gif|left|200px]]<br /><applet load="1nt0" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1nt0.gif|left|200px]]<br /><applet load="1nt0" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1nt0, resolution 2.70&Aring;" />
caption="1nt0, resolution 2.70&Aring;" />
'''Crystal structure of the CUB1-EGF-CUB2 region of MASP2'''<br />
'''Crystal structure of the CUB1-EGF-CUB2 region of MASP2'''<br />
==Overview==
==Overview==
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Serum mannose-binding proteins (MBPs) are C-type lectins that recognize, cell surface carbohydrate structures on pathogens, and trigger killing of, these targets by activating the complement pathway. MBPs circulate as a, complex with MBP-associated serine proteases (MASPs), which become, activated upon engagement of a target cell surface. The minimal functional, unit for complement activation is a MASP homodimer bound to two MBP, trimeric subunits. MASPs have a modular structure consisting of an, N-terminal CUB domain, a Ca(2+)-binding EGF-like domain, a second CUB, domain, two complement control protein modules and a C-terminal serine, protease domain. The CUB1-EGF-CUB2 region mediates homodimerization and, binding to MBP. The crystal structure of the MASP-2 CUB1-EGF-CUB2 dimer, reveals an elongated structure with a prominent concave surface that is, proposed to be the MBP-binding site. A model of the full six-domain, structure and its interaction with MBPs suggests mechanisms by which, binding to a target cell transmits conformational changes from MBP to MASP, that allow activation of its protease activity.
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Serum mannose-binding proteins (MBPs) are C-type lectins that recognize cell surface carbohydrate structures on pathogens, and trigger killing of these targets by activating the complement pathway. MBPs circulate as a complex with MBP-associated serine proteases (MASPs), which become activated upon engagement of a target cell surface. The minimal functional unit for complement activation is a MASP homodimer bound to two MBP trimeric subunits. MASPs have a modular structure consisting of an N-terminal CUB domain, a Ca(2+)-binding EGF-like domain, a second CUB domain, two complement control protein modules and a C-terminal serine protease domain. The CUB1-EGF-CUB2 region mediates homodimerization and binding to MBP. The crystal structure of the MASP-2 CUB1-EGF-CUB2 dimer reveals an elongated structure with a prominent concave surface that is proposed to be the MBP-binding site. A model of the full six-domain structure and its interaction with MBPs suggests mechanisms by which binding to a target cell transmits conformational changes from MBP to MASP that allow activation of its protease activity.
==About this Structure==
==About this Structure==
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1NT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with NAG, CA and EDO as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1NT0 OCA].
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1NT0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=EDO:'>EDO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NT0 OCA].
==Reference==
==Reference==
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Davies, J.M.]]
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[[Category: Davies, J M.]]
[[Category: Drickamer, K.]]
[[Category: Drickamer, K.]]
[[Category: Feinberg, H.]]
[[Category: Feinberg, H.]]
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[[Category: Uitdehaag, J.C.M.]]
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[[Category: Uitdehaag, J C.M.]]
[[Category: Wallis, R.]]
[[Category: Wallis, R.]]
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[[Category: Weis, W.I.]]
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[[Category: Weis, W I.]]
[[Category: CA]]
[[Category: CA]]
[[Category: EDO]]
[[Category: EDO]]
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[[Category: masp]]
[[Category: masp]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 22:31:50 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:09:38 2008''

Revision as of 12:09, 21 February 2008


1nt0, resolution 2.70Å

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Crystal structure of the CUB1-EGF-CUB2 region of MASP2

Overview

Serum mannose-binding proteins (MBPs) are C-type lectins that recognize cell surface carbohydrate structures on pathogens, and trigger killing of these targets by activating the complement pathway. MBPs circulate as a complex with MBP-associated serine proteases (MASPs), which become activated upon engagement of a target cell surface. The minimal functional unit for complement activation is a MASP homodimer bound to two MBP trimeric subunits. MASPs have a modular structure consisting of an N-terminal CUB domain, a Ca(2+)-binding EGF-like domain, a second CUB domain, two complement control protein modules and a C-terminal serine protease domain. The CUB1-EGF-CUB2 region mediates homodimerization and binding to MBP. The crystal structure of the MASP-2 CUB1-EGF-CUB2 dimer reveals an elongated structure with a prominent concave surface that is proposed to be the MBP-binding site. A model of the full six-domain structure and its interaction with MBPs suggests mechanisms by which binding to a target cell transmits conformational changes from MBP to MASP that allow activation of its protease activity.

About this Structure

1NT0 is a Single protein structure of sequence from Rattus norvegicus with , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of the CUB1-EGF-CUB2 region of mannose-binding protein associated serine protease-2., Feinberg H, Uitdehaag JC, Davies JM, Wallis R, Drickamer K, Weis WI, EMBO J. 2003 May 15;22(10):2348-59. PMID:12743029

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