1f58: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
New page: left|200px<br /> <applet load="1f58" size="450" color="white" frame="true" align="right" spinBox="true" caption="1f58, resolution 2.00Å" /> '''IGG1 FAB FRAGMENT (...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,328,572 edits
No edit summary
 
(17 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1f58.gif|left|200px]]<br />
<applet load="1f58" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1f58, resolution 2.00&Aring;" />
'''IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 24-RESIDUE PEPTIDE (RESIDUES 308-333 OF HIV-1 GP120 (MN ISOLATE) WITH ALA TO AIB SUBSTITUTION AT POSITION 323'''<br />


==Overview==
==IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 24-RESIDUE PEPTIDE (RESIDUES 308-333 OF HIV-1 GP120 (MN ISOLATE) WITH ALA TO AIB SUBSTITUTION AT POSITION 323==
BACKGROUND: The third hypervariable (V3) loop of HIV-1 gp120 has been, termed the principal neutralizing determinant (PND) of the virus and is, involved in many aspects of virus infectivity. The V3 loop is required for, viral entry into the cell via membrane fusion and is believed to interact, with cell surface chemokine receptors on T cells and macrophages. Sequence, changes in V3 can affect chemokine receptor usage, and can, therefore, modulate which types of cells are infected. Antibodies raised against, peptides with V3 sequences can neutralize laboratory-adapted strains of, the virus and inhibit syncytia formation. Fab fragments of these, neutralizing antibodies in complex with V3 loop peptides have been studied, by X-ray crystallography to determine the conformation of the V3 loop., RESULTS: We have determined three crystal structures of Fab 58.2, a, broadly neutralizing antibody, in complex with one linear and two cyclic, peptides the amino acid sequence of which comes from the MN isolate of the, gp120 V3 loop. Although the peptide conformations are very similar for the, linear and cyclic forms, they differ from that seen for the identical, peptide bound to a different broadly neutralizing antibody, Fab 59.1, and, for a similar peptide bound to the MN-specific Fab 50.1. The, conformational difference in the peptide is localized around residues, Gly-Pro-Gly-Arg, which are highly conserved in different HIV-1 isolates, and are predicted to adopt a type II beta turn. CONCLUSIONS: The V3 loop, can adopt at least two different conformations for the highly conserved, Gly-Pro-Gly-Arg sequence at the tip of the loop. Thus, the HIV-1 V3 loop, has some inherent conformational flexibility that may relate to its, biological function.
<StructureSection load='1f58' size='340' side='right'caption='[[1f58]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1f58]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/HIV-1_M:B_MN HIV-1 M:B_MN] and [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F58 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F58 FirstGlance]. <br>
</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&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AIB:ALPHA-AMINOISOBUTYRIC+ACID'>AIB</scene></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=1f58 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f58 OCA], [https://pdbe.org/1f58 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f58 RCSB], [https://www.ebi.ac.uk/pdbsum/1f58 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f58 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/KV3AE_MOUSE KV3AE_MOUSE]
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f5/1f58_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</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=1f58 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1F58 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1F58 OCA].
*[[Antibody 3D structures|Antibody 3D structures]]
 
*[[3D structures of non-human antibody|3D structures of non-human antibody]]
==Reference==
__TOC__
Dual conformations for the HIV-1 gp120 V3 loop in complexes with different neutralizing fabs., Stanfield R, Cabezas E, Satterthwait A, Stura E, Profy A, Wilson I, Structure. 1999 Feb 15;7(2):131-42. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10368281 10368281]
</StructureSection>
[[Category: HIV-1 M:B_MN]]
[[Category: Large Structures]]
[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Protein complex]]
[[Category: Cabezas E]]
[[Category: Cabezas, E.]]
[[Category: Profy AT]]
[[Category: Profy, A.T.]]
[[Category: Satterthwait AC]]
[[Category: Satterthwait, A.C.]]
[[Category: Stanfield RL]]
[[Category: Stanfield, R.L.]]
[[Category: Stura EA]]
[[Category: Stura, E.A.]]
[[Category: Wilson IA]]
[[Category: Wilson, I.A.]]
[[Category: fab]]
[[Category: gp120]]
[[Category: hiv-1]]
[[Category: immunoglobulin]]
[[Category: v3]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov  8 14:02:13 2007''

Latest revision as of 10:10, 20 March 2024

IGG1 FAB FRAGMENT (58.2) COMPLEX WITH 24-RESIDUE PEPTIDE (RESIDUES 308-333 OF HIV-1 GP120 (MN ISOLATE) WITH ALA TO AIB SUBSTITUTION AT POSITION 323

1f58, resolution 2.00Å

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1f58&oldid=4108705"