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| <StructureSection load='1cl7' size='340' side='right'caption='[[1cl7]], [[Resolution|resolution]] 3.00Å' scene=''> | | <StructureSection load='1cl7' size='340' side='right'caption='[[1cl7]], [[Resolution|resolution]] 3.00Å' scene=''> |
| == Structural highlights == | | == Structural highlights == |
- | <table><tr><td colspan='2'>[[1cl7]] is a 3 chain structure with sequence 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=1CL7 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CL7 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1cl7]] is a 3 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=1CL7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CL7 FirstGlance]. <br> |
- | </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=1cl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cl7 OCA], [http://pdbe.org/1cl7 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cl7 RCSB], [http://www.ebi.ac.uk/pdbsum/1cl7 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cl7 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]] 3Å</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=1cl7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cl7 OCA], [https://pdbe.org/1cl7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cl7 RCSB], [https://www.ebi.ac.uk/pdbsum/1cl7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cl7 ProSAT]</span></td></tr> |
| </table> | | </table> |
| + | == Function == |
| + | [https://www.uniprot.org/uniprot/IGH1M_MOUSE IGH1M_MOUSE] |
| == Evolutionary Conservation == | | == Evolutionary Conservation == |
| [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| ==See Also== | | ==See Also== |
| *[[Antibody 3D structures|Antibody 3D structures]] | | *[[Antibody 3D structures|Antibody 3D structures]] |
| + | *[[Sandbox 20009|Sandbox 20009]] |
| + | *[[3D structures of non-human antibody|3D structures of non-human antibody]] |
| == References == | | == References == |
| <references/> | | <references/> |
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| [[Category: Large Structures]] | | [[Category: Large Structures]] |
| [[Category: Mus musculus]] | | [[Category: Mus musculus]] |
- | [[Category: Bentley, G A]] | + | [[Category: Bentley GA]] |
- | [[Category: Lescar, J]] | + | [[Category: Lescar J]] |
- | [[Category: Cross-reactivity]]
| + | |
- | [[Category: Enzyme inhibition]]
| + | |
- | [[Category: Fab fragment]]
| + | |
- | [[Category: Hiv1 protease]]
| + | |
- | [[Category: Immune system]]
| + | |
- | [[Category: Immunoglobulin]]
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| Structural highlights
Function
IGH1M_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 monoclonal antibody 1696, directed against the HIV-1 protease, displays strong inhibitory effects toward the catalytic activity of the enzyme of both the HIV-1 and HIV-2 isolates. This antibody cross-reacts with peptides that include the N-terminus of the enzyme, a region that is well conserved in sequence among different viral strains and which, furthermore, is crucial for homodimerization to the active enzymatic form. This observation, as well as antigen-binding studies in the presence of an active site inhibitor, suggest that 1696 inhibits the HIV protease by destabilizing its active homodimeric form. To characterize further how the antibody 1696 inhibits the HIV-1 and HIV-2 proteases, we have solved the crystal structure of its Fab fragment by molecular replacement and refined it at 3.0 A resolution. The antigen binding site has a deep cavity at its center, which is lined mainly by acidic and hydrophobic residues, and is large enough to accommodate several antigen residues. The structure of the Fab 1696 could form a starting basis for the design of alternative HIV protease-inhibiting molecules of broad specificity.
Inhibition of the HIV-1 and HIV-2 proteases by a monoclonal antibody.,Lescar J, Brynda J, Rezacova P, Stouracova R, Riottot MM, Chitarra V, Fabry M, Horejsi M, Sedlacek J, Bentley GA Protein Sci. 1999 Dec;8(12):2686-96. PMID:10631984[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Lescar J, Brynda J, Rezacova P, Stouracova R, Riottot MM, Chitarra V, Fabry M, Horejsi M, Sedlacek J, Bentley GA. Inhibition of the HIV-1 and HIV-2 proteases by a monoclonal antibody. Protein Sci. 1999 Dec;8(12):2686-96. PMID:10631984
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