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1k5m

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(New page: 200px<br /> <applet load="1k5m" size="450" color="white" frame="true" align="right" spinBox="true" caption="1k5m, resolution 2.7&Aring;" /> '''Crystal Structure of...)
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[[Image:1k5m.gif|left|200px]]<br />
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[[Image:1k5m.gif|left|200px]]<br /><applet load="1k5m" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1k5m" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1k5m, resolution 2.7&Aring;" />
caption="1k5m, resolution 2.7&Aring;" />
'''Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2'''<br />
'''Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2'''<br />
==Overview==
==Overview==
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We report the 2.7 A resolution structure of a chimeric rhinovirus, MN-III-2, that displays part of the HIV-1 gp120 V3 loop and elicits, HIV-neutralizing antibodies. The V3 loop insert is dominated by two type I, beta turns. The structures of two adjacent tripeptides resemble those of, analogous segments in three Fab/V3 loop peptide complexes. Although two of, the three corresponding antibodies bind and neutralize MN-III-2 well, only, one of the three can bind without significant rearrangement. These results, suggest that the V3 loop insert: (1) can share some local conformational, similarity to V3 loop sequences presented on different structural, frameworks; (2) must be able to adopt multiple conformations, even in a, relatively constrained environment; and (3) may mimic the conformational, variability of the epitope on HIV-1, increasing the likelihood of, eliciting appropriate neutralizing immune responses.
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We report the 2.7 A resolution structure of a chimeric rhinovirus, MN-III-2, that displays part of the HIV-1 gp120 V3 loop and elicits HIV-neutralizing antibodies. The V3 loop insert is dominated by two type I beta turns. The structures of two adjacent tripeptides resemble those of analogous segments in three Fab/V3 loop peptide complexes. Although two of the three corresponding antibodies bind and neutralize MN-III-2 well, only one of the three can bind without significant rearrangement. These results suggest that the V3 loop insert: (1) can share some local conformational similarity to V3 loop sequences presented on different structural frameworks; (2) must be able to adopt multiple conformations, even in a relatively constrained environment; and (3) may mimic the conformational variability of the epitope on HIV-1, increasing the likelihood of eliciting appropriate neutralizing immune responses.
==About this Structure==
==About this Structure==
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1K5M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_rhinovirus_10 Human rhinovirus 10] with SPH as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1K5M OCA].
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1K5M is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Human_rhinovirus_10 Human rhinovirus 10] with <scene name='pdbligand=SPH:'>SPH</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K5M OCA].
==Reference==
==Reference==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Arnold, E.]]
[[Category: Arnold, E.]]
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[[Category: Arnold, G.F.]]
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[[Category: Arnold, G F.]]
[[Category: Ding, J.]]
[[Category: Ding, J.]]
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[[Category: Geisler, S.C.]]
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[[Category: Geisler, S C.]]
[[Category: Ma, X.]]
[[Category: Ma, X.]]
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[[Category: Smith, A.D.]]
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[[Category: Smith, A D.]]
[[Category: SPH]]
[[Category: SPH]]
[[Category: beta turns]]
[[Category: beta turns]]
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[[Category: icosahedral virus]]
[[Category: icosahedral virus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:15:03 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:30:28 2008''

Revision as of 11:30, 21 February 2008


1k5m, resolution 2.7Å

Drag the structure with the mouse to rotate

Crystal Structure of a Human Rhinovirus Type 14:Human Immunodeficiency Virus Type 1 V3 Loop Chimeric Virus MN-III-2

Overview

We report the 2.7 A resolution structure of a chimeric rhinovirus, MN-III-2, that displays part of the HIV-1 gp120 V3 loop and elicits HIV-neutralizing antibodies. The V3 loop insert is dominated by two type I beta turns. The structures of two adjacent tripeptides resemble those of analogous segments in three Fab/V3 loop peptide complexes. Although two of the three corresponding antibodies bind and neutralize MN-III-2 well, only one of the three can bind without significant rearrangement. These results suggest that the V3 loop insert: (1) can share some local conformational similarity to V3 loop sequences presented on different structural frameworks; (2) must be able to adopt multiple conformations, even in a relatively constrained environment; and (3) may mimic the conformational variability of the epitope on HIV-1, increasing the likelihood of eliciting appropriate neutralizing immune responses.

About this Structure

1K5M is a Protein complex structure of sequences from Human rhinovirus 10 with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a human rhinovirus that displays part of the HIV-1 V3 loop and induces neutralizing antibodies against HIV-1., Ding J, Smith AD, Geisler SC, Ma X, Arnold GF, Arnold E, Structure. 2002 Jul;10(7):999-1011. PMID:12121655

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