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==STRUCTURE OF THE SINGLE-DOMAIN CAMELID ANTIBODY CAB-CA05== | |||
<StructureSection load='1f2x' size='340' side='right'caption='[[1f2x]], [[Resolution|resolution]] 2.10Å' scene=''> | |||
| | == Structural highlights == | ||
| | <table><tr><td colspan='2'>[[1f2x]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Camelus_dromedarius Camelus dromedarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F2X FirstGlance]. <br> | ||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</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=1f2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f2x OCA], [https://pdbe.org/1f2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f2x RCSB], [https://www.ebi.ac.uk/pdbsum/1f2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f2x ProSAT]</span></td></tr> | |||
</table> | |||
== 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/f2/1f2x_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=1f2x ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Grafting the antigen-binding loops onto a human antibody scaffold is a widely used technique to humanise murine antibodies. The success of this approach depends largely on the observation that the antigen-binding loops adopt only a limited number of canonical structures. Identification of the correct canonical structure is therefore essential. Algorithms that predict the main-chain conformation of the hypervariable loops using only the amino acid sequence often provide this information. Here, we describe new canonical loop conformations for the hypervariable regions H1 and H2 as found in single-domain antibody fragments of dromedaries or llama. Although the occurrence of these new loop conformations was not predicted by the algorithms used, it seems that they could occur in human or mouse antigen-binding loops. Their discovery indicates that the currently used set of canonical structures is incomplete and that the prediction algorithms should be extended to include these new structures. | |||
Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?,Decanniere K, Muyldermans S, Wyns L J Mol Biol. 2000 Jun 30;300(1):83-91. PMID:10864500<ref>PMID:10864500</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1f2x" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
*[[Antibody 3D structures|Antibody 3D structures]] | |||
*[[3D structures of non-human antibody|3D structures of non-human antibody]] | |||
== | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Camelus dromedarius]] | [[Category: Camelus dromedarius]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Decanniere | [[Category: Decanniere K]] | ||
[[Category: Muyldermans | [[Category: Muyldermans S]] | ||
[[Category: Wyns | [[Category: Wyns L]] | ||
Latest revision as of 09:36, 30 October 2024
STRUCTURE OF THE SINGLE-DOMAIN CAMELID ANTIBODY CAB-CA05STRUCTURE OF THE SINGLE-DOMAIN CAMELID ANTIBODY CAB-CA05
Structural highlights
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 PubMedGrafting the antigen-binding loops onto a human antibody scaffold is a widely used technique to humanise murine antibodies. The success of this approach depends largely on the observation that the antigen-binding loops adopt only a limited number of canonical structures. Identification of the correct canonical structure is therefore essential. Algorithms that predict the main-chain conformation of the hypervariable loops using only the amino acid sequence often provide this information. Here, we describe new canonical loop conformations for the hypervariable regions H1 and H2 as found in single-domain antibody fragments of dromedaries or llama. Although the occurrence of these new loop conformations was not predicted by the algorithms used, it seems that they could occur in human or mouse antigen-binding loops. Their discovery indicates that the currently used set of canonical structures is incomplete and that the prediction algorithms should be extended to include these new structures. Canonical antigen-binding loop structures in immunoglobulins: more structures, more canonical classes?,Decanniere K, Muyldermans S, Wyns L J Mol Biol. 2000 Jun 30;300(1):83-91. PMID:10864500[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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