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Contents |
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339 a.a.
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175 a.a.
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215 a.a.
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233 a.a.
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* Residue conservation analysis
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PDB id:
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Viral protein/immune system
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Title:
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Crystal structure of HIV-1 jr-fl gp120 core protein containing the third variable region (v3) complexed with cd4 and the x5 antibody
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Structure:
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Envelope glycoprotein. Chain: g. Fragment: core with v3. Engineered: yes. Mutation: yes. T-cell surface glycoprotein cd4. Chain: c. Fragment: d1d2, n-terminal two domain fragment. Synonym: t-cell surface antigen t4/leu-3.
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Source:
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Human immunodeficiency virus 1. Organism_taxid: 11676. Expressed in: drosophila melanogaster. Expression_system_taxid: 7227. Homo sapiens. Human. Organism_taxid: 9606. Gene: cd4. Expressed in: cricetulus griseus.
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Biol. unit:
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Tetramer (from
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Resolution:
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3.30Å
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R-factor:
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0.319
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R-free:
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0.349
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Authors:
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C.Huang,M.Tang,M.Y.Zhang,S.Majeed,E.Montabana,R.L.Stanfield, D.S.Dimitrov,B.Korber,J.Sodroski,I.A.Wilson,R.Wyatt,P.D.Kwong
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Key ref:
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C.C.Huang
et al.
(2005).
Structure of a V3-containing HIV-1 gp120 core.
Science,
310,
1025-1028.
PubMed id:
DOI:
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Date:
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23-Sep-05
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Release date:
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15-Nov-05
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PROCHECK
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Headers
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References
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Q75760
(Q75760_HV1) -
Envelope glycoprotein gp160 from Human immunodeficiency virus type 1
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Seq:
Struc:
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847 a.a.
339 a.a.*
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P01730
(CD4_HUMAN) -
T-cell surface glycoprotein CD4 from Homo sapiens
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Seq:
Struc:
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458 a.a.
175 a.a.
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DOI no:
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Science
310:1025-1028
(2005)
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PubMed id:
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Structure of a V3-containing HIV-1 gp120 core.
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C.C.Huang,
M.Tang,
M.Y.Zhang,
S.Majeed,
E.Montabana,
R.L.Stanfield,
D.S.Dimitrov,
B.Korber,
J.Sodroski,
I.A.Wilson,
R.Wyatt,
P.D.Kwong.
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ABSTRACT
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The third variable region (V3) of the HIV-1 gp120 envelope glycoprotein is
immunodominant and contains features essential for coreceptor binding. We
determined the structure of V3 in the context of an HIV-1 gp120 core complexed
to the CD4 receptor and to the X5 antibody at 3.5 angstrom resolution. Binding
of gp120 to cell-surface CD4 would position V3 so that its coreceptor-binding
tip protrudes 30 angstroms from the core toward the target cell membrane. The
extended nature and antibody accessibility of V3 explain its immunodominance.
Together, the results provide a structural rationale for the role of V3 in HIV
entry and neutralization.
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Selected figure(s)
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Figure 1.
Fig. 1. Structure of an HIV-1 gp120 core with V3. The crystal
structure of core gp120 (gray) with an intact V3 (red) is shown
bound to the membrane-distal two domains of the CD4 receptor
(yellow) and the Fab portion of the X5 antibody (dark and light
blue). In this orientation, the viral membrane would be
positioned toward the top of the page and the target cell toward
the bottom.
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Figure 3.
Fig. 3. Modeled trimer and coreceptor schematic. (A) V3 in the
context of a trimer at the target cell surface. The structure of
the CD4-triggered gp120 with V3 was superimposed onto the
structure of four-domain CD4 (39) and the trimer model obtained
by quantification of surface parameters (32). In this
orientation, the target cell membrane and coreceptor are
expected to be positioned toward the bottom of the page. (B)
Schematic of coreceptor interaction. CCR5 (green) is shown with
its tyrosine-sulfated N terminus (at residues 3, 10, 14, and 15)
and three extracellular loops (ECLs). V3 (red) is shown with its
conserved base interacting with the sulfated CCR5 N terminus and
its flexible legs allowing its conserved V3 tip to reach the
second ECL of CCR5.
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The above figures are
reprinted
by permission from the AAAs:
Science
(2005,
310,
1025-1028)
copyright 2005.
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Figures were
selected
by an automated process.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.Emileh,
and
C.F.Abrams
(2011).
A mechanism by which binding of the broadly neutralizing antibody b12 unfolds the inner domain α1 helix in an engineered HIV-1 gp120.
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Proteins,
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and
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Some binding-related drug properties are dependent on thermodynamic signature.
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Chem Biol Drug Des,
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B.Wei,
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Use of mutual information arrays to predict coevolving sites in the full length HIV gp120 protein for subtypes B and C.
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Virol Sin,
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PDB codes:
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L.T.Da,
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PDB codes:
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PDB code:
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PDB codes:
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P.Lusso
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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| |
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