1fai: Difference between revisions

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{{Seed}}
[[Image:1fai.png|left|200px]]


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==THREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODY==
The line below this paragraph, containing "STRUCTURE_1fai", creates the "Structure Box" on the page.
<StructureSection load='1fai' size='340' side='right'caption='[[1fai]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1fai]] 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=1FAI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FAI FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fai FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fai OCA], [https://pdbe.org/1fai PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fai RCSB], [https://www.ebi.ac.uk/pdbsum/1fai PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fai ProSAT]</span></td></tr>
{{STRUCTURE_1fai|  PDB=1fai  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_MOUSE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fa/1fai_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1fai ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and II) to a resolution of 2.8 and 2.7 A, respectively. Essentially the same tertiary and quaternary structure of the Fab is observed in the two forms. The major difference resides in the intermolecular contacts, which are interpreted to favor an irreversible transition from the metastable form I to the more stable form II. The third complementarity-determining region of the heavy chain (H3) folds back over the combining site and requires rearrangement for hapten binding. This dynamic requirement on H3 is consistent with its mobility in the structure and can explain hapten binding to an otherwise inaccessible antibody combining site.


===THREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODY===
Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody.,Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9429-33. PMID:1409652<ref>PMID:1409652</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fai" style="background-color:#fffaf0;"></div>


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==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_1409652}}, adds the Publication Abstract to the page
*[[Monoclonal Antibodies 3D structures|Monoclonal Antibodies 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 1409652 is the PubMed ID number.
== References ==
-->
<references/>
{{ABSTRACT_PUBMED_1409652}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
1FAI is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FAI OCA].
 
==Reference==
<ref group="xtra">PMID:1409652</ref><references group="xtra"/>
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Alzari, P M.]]
[[Category: Alzari PM]]
[[Category: Lascombe, M B.]]
[[Category: Lascombe MB]]
[[Category: Nisonoff, A.]]
[[Category: Nisonoff A]]
[[Category: Poljak, R J.]]
[[Category: Poljak RJ]]
[[Category: Immunoglobulin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Sep 21 19:35:42 2009''

Latest revision as of 02:58, 21 November 2024

THREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODYTHREE-DIMENSIONAL STRUCTURE OF TWO CRYSTAL FORMS OF FAB R19.9, FROM A MONOCLONAL ANTI-ARSONATE ANTIBODY

Structural highlights

1fai 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 diffraction, Resolution 2.7Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

IGKC_MOUSE

Evolutionary Conservation

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

Publication Abstract from PubMed

The three-dimensional structure of FabR19.9 from a well-characterized anti-p-azobenzenearsonate monoclonal antibody has been determined by x-ray diffraction techniques in two crystalline forms (I and II) to a resolution of 2.8 and 2.7 A, respectively. Essentially the same tertiary and quaternary structure of the Fab is observed in the two forms. The major difference resides in the intermolecular contacts, which are interpreted to favor an irreversible transition from the metastable form I to the more stable form II. The third complementarity-determining region of the heavy chain (H3) folds back over the combining site and requires rearrangement for hapten binding. This dynamic requirement on H3 is consistent with its mobility in the structure and can explain hapten binding to an otherwise inaccessible antibody combining site.

Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody.,Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9429-33. PMID:1409652[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. Lascombe MB, Alzari PM, Poljak RJ, Nisonoff A. Three-dimensional structure of two crystal forms of FabR19.9 from a monoclonal anti-arsonate antibody. Proc Natl Acad Sci U S A. 1992 Oct 15;89(20):9429-33. PMID:1409652

1fai, resolution 2.70Å

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