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| - | [[Image:1mf2.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1mf2| PDB=1mf2 | SCENE= }} | | {{STRUCTURE_1mf2| PDB=1mf2 | SCENE= }} |
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| - | '''ANTI HIV1 PROTEASE FAB COMPLEX'''
| + | ===ANTI HIV1 PROTEASE FAB COMPLEX=== |
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| - | ==Overview==
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| - | F11.2.32, a monoclonal antibody raised against HIV-1 protease (Kd = 5 nM), which inhibits proteolytic activity of the enzyme (K(inh) = 35(+/-3)nM), has been studied by crystallographic methods. The three-dimensional structure of the complex between the Fab fragment and a synthetic peptide, spanning residues 36 to 46 of the protease, has been determined at 2.2 A resolution, and that of the Fab in the free state has been determined at 2.6 A resolution. The refined model of the complex reveals ten well-ordered residues of the peptide (P36 to P45) bound in a hydrophobic cavity at the centre of the antigen-binding site. The peptide adopts a beta hairpin-like structure in which residues P38 to P42 form a type II beta-turn conformation. An intermolecular antiparallel beta-sheet is formed between the peptide and the CDR3-H loop of the antibody; additional polar interactions occur between main-chain atoms of the peptide and hydroxyl groups from tyrosine residues protruding from CDR1-L and CDR3-H. Three water molecules, located at the antigen-antibody interface, mediate polar interactions between the peptide and the most buried hypervariable loops, CDR3-L and CDR1-H. A comparison between the free and complexed Fab fragments shows that significant conformational changes occur in the long hypervariable regions, CDR1-L and CDR3-H, upon binding the peptide. The conformation of the bound peptide, which shows no overall structural similarity to the corresponding segment in HIV-1 protease, suggests that F11.2.32 might inhibit proteolysis by distorting the native structure of the enzyme.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_9150407}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9150407 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9150407}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Hiv1 protease]] | | [[Category: Hiv1 protease]] |
| | [[Category: Immunoglobulin]] | | [[Category: Immunoglobulin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:57:30 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:49:47 2008'' |
Revision as of 20:49, 2 July 2008
Template:STRUCTURE 1mf2
ANTI HIV1 PROTEASE FAB COMPLEX
Template:ABSTRACT PUBMED 9150407
About this Structure
1MF2 is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of an Fab-peptide complex: structural basis of HIV-1 protease inhibition by a monoclonal antibody., Lescar J, Stouracova R, Riottot MM, Chitarra V, Brynda J, Fabry M, Horejsi M, Sedlacek J, Bentley GA, J Mol Biol. 1997 Apr 18;267(5):1207-22. PMID:9150407
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