1ntl: Difference between revisions

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==Model of mouse Crry-Ig determined by solution scattering, curve fitting and homology modelling==
==Model of mouse Crry-Ig determined by solution scattering, curve fitting and homology modelling==
<StructureSection load='1ntl' size='340' side='right' caption='[[1ntl]], [[Resolution|resolution]] 30.00&Aring;' scene=''>
<StructureSection load='1ntl' size='340' side='right'caption='[[1ntl]], [[Resolution|resolution]] 30.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1ntl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NTL OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1NTL FirstGlance]. <br>
<table><tr><td colspan='2'>[[1ntl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NTL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1NTL FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1qub|1qub]], [[1gkg|1gkg]], [[1ckl|1ckl]], [[1vvc|1vvc]], [[1igy|1igy]]</td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray solution scattering, [[Resolution|Resolution]] 30&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ntl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ntl OCA], [http://pdbe.org/1ntl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ntl RCSB], [http://www.ebi.ac.uk/pdbsum/1ntl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ntl ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ntl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ntl OCA], [https://pdbe.org/1ntl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ntl RCSB], [https://www.ebi.ac.uk/pdbsum/1ntl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ntl ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[[http://www.uniprot.org/uniprot/CR1L_MOUSE CR1L_MOUSE]] Acts as a cofactor for complement factor I, a serine protease which protects autologous cells against complement-mediated injury by cleaving C3b and C4b deposited on host tissue. Also acts as a decay-accelerating factor, preventing the formation of C4b2a and C3bBb, the amplification convertases of the complement cascade. Plays a crucial role in early embryonic development by maintaining fetomaternal tolerance. Also acts as a costimulatory factor for T-cells which favors IL-4 secretion.<ref>PMID:1730912</ref> <ref>PMID:7528766</ref> <ref>PMID:10779754</ref> <ref>PMID:10642554</ref> <ref>PMID:11986227</ref> 
[https://www.uniprot.org/uniprot/IGHG1_MOUSE IGHG1_MOUSE]  
== Evolutionary Conservation ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/1ntl_consurf.spt"</scriptWhenChecked>
     <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/nt/1ntl_consurf.spt"</scriptWhenChecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
Line 19: Line 19:
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ntl ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ntl ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Complement receptor-related gene/protein y (Crry) is a cell membrane-bound regulator of complement activation found in mouse and rat. Crry contains only short complement/consensus repeat (SCR) domains. X-ray and neutron scattering was performed on recombinant rat Crry containing the first five SCR domains (rCrry) and mouse Crry with five SCR domains conjugated to the Fc fragment of mouse IgG1 (mCrry-Ig) in order to determine their solution structures at medium resolution. The radius of gyration R(G) of rCrry was determined to be 4.9-5.0 nm, and the R(G) of the cross-section was 1.2-1.5 nm as determined by X-ray and neutron scattering. The R(G) of mCrry-Ig was 6.6-6.7 nm, and the R(G) of the cross-section were 2.3-2.4 nm and 1.3 nm. The maximum dimension of rCrry was 18 nm and that for mCrry-Ig was 26 nm. The neutron data indicated that rCrry and mCrry-Ig have molecular mass values of 45,000 Da and 140,000 Da, respectively, in agreement with their sequences, and sedimentation equilibrium data supported these determinations. Time-derivative velocity experiments gave sedimentation coefficients of 2.4S for rCrry and 5.4S for mCrry-Ig. A medium-resolution model of rCrry was determined using homology models that were constructed for the first five SCR domains of Crry from known crystal and NMR structures, and linked by randomly generated linker peptide conformations. These trial-and-error calculations revealed a small family of extended rCrry structures that best accounted for the scattering and ultracentrifugation data. These were shorter than the most extended rCrry models as the result of minor bends in the inter-SCR orientations. The mCrry-Ig solution data were modelled starting from a fixed structure for rCrry and the crystal structure of mouse IgG1, and was based on conformational searches of the hinge peptide joining the mCrry and Fc fragments. The best-fit models showed that the two mCrry antennae in mCrry-Ig were extended from the Fc fragment. No preferred orientation of the antennae was identified, and this indicated that the accessibility of the antennae for the molecular targets C4b and C3b was not affected by the covalent link to Fc. A structural comparison between Crry and complement receptor type 1 indicated that the domain arrangement of Crry SCR 1-3 is as extended as that of the CR1 SCR 15-17 NMR structure.
The extended multidomain solution structures of the complement protein Crry and its chimeric conjugate Crry-Ig by scattering, analytical ultracentrifugation and constrained modelling: implications for function and therapy.,Aslam M, Guthridge JM, Hack BK, Quigg RJ, Holers VM, Perkins SJ J Mol Biol. 2003 Jun 6;329(3):525-50. PMID:12767833<ref>PMID:12767833</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1ntl" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Lk3 transgenic mice]]
[[Category: Large Structures]]
[[Category: Aslam, M]]
[[Category: Mus musculus]]
[[Category: Guthridge, J M]]
[[Category: Aslam M]]
[[Category: Hack, B K]]
[[Category: Guthridge JM]]
[[Category: Holers, V M]]
[[Category: Hack BK]]
[[Category: Perkins, S J]]
[[Category: Holers VM]]
[[Category: Quigg, R J]]
[[Category: Perkins SJ]]
[[Category: Ccp]]
[[Category: Quigg RJ]]
[[Category: Complement]]
[[Category: Glycoprotein]]
[[Category: Immune system]]
[[Category: Immunology]]
[[Category: Scr]]

Latest revision as of 10:59, 14 February 2024

Model of mouse Crry-Ig determined by solution scattering, curve fitting and homology modellingModel of mouse Crry-Ig determined by solution scattering, curve fitting and homology modelling

Structural highlights

1ntl is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray solution scattering, Resolution 30Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IGHG1_MOUSE

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

1ntl, resolution 30.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA
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