1jpt: Difference between revisions

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<StructureSection load='1jpt' size='340' side='right'caption='[[1jpt]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
<StructureSection load='1jpt' size='340' side='right'caption='[[1jpt]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1jpt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JPT FirstGlance]. <br>
<table><tr><td colspan='2'>[[1jpt]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JPT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JPT FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1jps|1jps]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.85&#8491;</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=1jpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jpt OCA], [https://pdbe.org/1jpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jpt RCSB], [https://www.ebi.ac.uk/pdbsum/1jpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jpt 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=1jpt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jpt OCA], [https://pdbe.org/1jpt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jpt RCSB], [https://www.ebi.ac.uk/pdbsum/1jpt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jpt ProSAT]</span></td></tr>
</table>
</table>
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</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=1jpt 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=1jpt ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The outstanding importance of the antigen-antibody recognition process for the survival and defence strategy of higher organisms is in sharp contrast to the limited high resolution structural data available on antibody-antigen pairs with antigenic proteins. The limitation is the most severe for structural data not restricted to the antigen-antibody complex but extending to the uncomplexed antigen and antibody. We report the crystal structure of the complex between tissue factor (TF) and the humanized Fab fragment D3h44 at a resolution of 1.85 A together with the structure of uncomplexed D3h44 at the same resolution. In conjunction with the previously reported 1.7 A crystal structure of uncomplexed TF, a unique opportunity is generated to explore details of the recognition process. The TF.D3h44 interface is characterised by a high number of polar interactions, including as may as 46 solvent molecules. Conformational changes upon complex formation are very small and almost exclusively limited to the reorientation of side-chains. The binding epitope is in complete agreement with earlier mutagenesis experiments. A revaluation of two other antibody-antigen pairs reported at similar resolutions, shows that all these complexes are very similar with respect to the solvation of the interface, the number of solvent positions conserved in the uncomplexed and complexed proteins and the number of water molecules expelled from the surface and replaced by hydrophilic atoms from the binding partner upon complex formation. A strategy is proposed on how to exploit this high resolution structural data to guide the affinity maturation of humanised antibodies.
The 1.85 A resolution crystal structures of tissue factor in complex with humanized Fab D3h44 and of free humanized Fab D3h44: revisiting the solvation of antigen combining sites.,Faelber K, Kirchhofer D, Presta L, Kelley RF, Muller YA J Mol Biol. 2001 Oct 12;313(1):83-97. PMID:11601848<ref>PMID:11601848</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1jpt" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
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*[[Sandbox 20009|Sandbox 20009]]
*[[Sandbox 20009|Sandbox 20009]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Human]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Faelber, K]]
[[Category: Faelber K]]
[[Category: Kelley, R F]]
[[Category: Kelley RF]]
[[Category: Kirchhofer, D]]
[[Category: Kirchhofer D]]
[[Category: Muller, Y A]]
[[Category: Muller YA]]
[[Category: Presta, L]]
[[Category: Presta L]]
[[Category: Antigen-antibody recognition]]
[[Category: Blood coagulation]]
[[Category: Humanized antibody]]
[[Category: Immune system]]

Revision as of 06:04, 3 April 2024

Crystal Structure of Fab D3H44

1jpt, resolution 1.85Å

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