From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1u6v.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1u6v.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1u6v| PDB=1u6v | SCENE= }} | | {{STRUCTURE_1u6v| PDB=1u6v | SCENE= }} |
| | | | |
| - | '''NMR structure of a V3 (IIIB isolate) peptide bound to 447-52D, a human HIV-1 neutralizing antibody'''
| + | ===NMR structure of a V3 (IIIB isolate) peptide bound to 447-52D, a human HIV-1 neutralizing antibody=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Human monoclonal antibody (mAb) 447-52D neutralizes a broad spectrum of HIV-1 isolates, whereas murine mAb 0.5beta, raised against gp120 of the X4 isolate HIV-1(IIIB), neutralizes this strain specifically. Two distinct gp120 V3 peptides, V3(MN) and V3(IIIB), adopt alternative beta-hairpin conformations when bound to 447-52D and 0.5beta, respectively, suggesting that the alternative conformations of this loop play a key role in determining the coreceptor specificity of HIV-1. To test this hypothesis and to better understand the molecular basis underlying an antibody's breadth of neutralization, the solution structure of the V3(IIIB) peptide bound to 447-52D was determined by NMR. V3(IIIB) and V3(MN) peptides bound to 447-52D exhibited the same N-terminal strand conformation, while the V3(IIIB) peptide revealed alternative N-terminal conformations when bound to 447-52D and 0.5beta. Comparison of the three known V3 structures leads to a model in which a 180 degrees change in the orientation of the side chains and the resulting one-residue shift in hydrogen bonding patterns in the N-terminal strand of the beta-hairpins markedly alter the topology of the surface that interacts with antibodies and that can potentially interact with the HIV-1 coreceptors. Predominant interactions of 447-52D with three conserved residues of the N-terminal side of the V3 loop, K312, I314, and I316, can account for its broad cross reactivity, whereas the predominant interactions of 0.5beta with variable residues underlie its strain specificity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15882063}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15882063 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15882063}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| - | Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U6V OCA]. | + | Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1U6V OCA]. |
| | | | |
| | ==Reference== | | ==Reference== |
| Line 28: |
Line 32: |
| | [[Category: Zolla-Pazner, S.]] | | [[Category: Zolla-Pazner, S.]] |
| | [[Category: Beta hairpin]] | | [[Category: Beta hairpin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:50:02 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 06:32:31 2008'' |
Revision as of 03:32, 28 July 2008
Template:STRUCTURE 1u6v
NMR structure of a V3 (IIIB isolate) peptide bound to 447-52D, a human HIV-1 neutralizing antibody
Template:ABSTRACT PUBMED 15882063
About this Structure
Full experimental information is available from OCA.
Reference
Induced fit in HIV-neutralizing antibody complexes: evidence for alternative conformations of the gp120 V3 loop and the molecular basis for broad neutralization., Rosen O, Chill J, Sharon M, Kessler N, Mester B, Zolla-Pazner S, Anglister J, Biochemistry. 2005 May 17;44(19):7250-8. PMID:15882063
Page seeded by OCA on Mon Jul 28 06:32:31 2008
