1cfq: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cfq]] 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=1CFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[1cfq]] 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=1CFQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFQ FirstGlance]. <br> | ||
</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=1cfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfq OCA], [https://pdbe.org/1cfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfq RCSB], [https://www.ebi.ac.uk/pdbsum/1cfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfq ProSAT]</span></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]] 2.8Å</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=1cfq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfq OCA], [https://pdbe.org/1cfq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfq RCSB], [https://www.ebi.ac.uk/pdbsum/1cfq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfq ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/IGKC_MOUSE IGKC_MOUSE] | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Hoehne | [[Category: Hoehne W]] | ||
[[Category: Keitel | [[Category: Keitel T]] | ||
[[Category: Kramer | [[Category: Kramer A]] | ||
[[Category: Schneider-Mergener | [[Category: Schneider-Mergener J]] | ||
[[Category: Scholz | [[Category: Scholz C]] | ||
[[Category: Wessner | [[Category: Wessner H]] | ||
Latest revision as of 02:26, 28 December 2023
ANTI-P24 (HIV-1) FAB FRAGMENT CB41ANTI-P24 (HIV-1) FAB FRAGMENT CB41
Structural highlights
FunctionEvolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe X-ray crystal structures of an anti-p24 (HIV-1) monoclonal antibody Fab fragment alone and in complexes with the epitope peptide GATPQDLNTnL (n = norleucine), an epitope-homologous peptide GATPEDLNQKLAGN, as well as two unrelated peptides GLYEWGGARITNTD and efslkGpllqwrsG (D-peptide), are presented to a maximum resolution of 2.6 A. The latter three peptides were identified from screening synthetic combinatorial peptide libraries. Although all peptides bind to the same antigen combining site, the nonhomologous peptides adopt different binding conformations and also form their critical contacts with different antibody residues. Only small readjustments are observed within the framework of the Fab fragment upon binding. Crystallographic analysis of anti-p24 (HIV-1) monoclonal antibody cross-reactivity and polyspecificity.,Keitel T, Kramer A, Wessner H, Scholz C, Schneider-Mergener J, Hohne W Cell. 1997 Dec 12;91(6):811-20. PMID:9413990[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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