1l6n

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(New page: 200px<br /> <applet load="1l6n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1l6n" /> '''STRUCTURE OF THE N-TERMINAL 283-RESIDUE FRA...)
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'''STRUCTURE OF THE N-TERMINAL 283-RESIDUE FRAGMENT OF THE HIV-1 GAG POLYPROTEIN'''<br />
'''STRUCTURE OF THE N-TERMINAL 283-RESIDUE FRAGMENT OF THE HIV-1 GAG POLYPROTEIN'''<br />
==Overview==
==Overview==
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The capsid protein (CA) of the mature human immunodeficiency virus (HIV), contains an N-terminal beta-hairpin that is essential for formation of the, capsid core particle. CA is generated by proteolytic cleavage of the Gag, precursor polyprotein during viral maturation. We have determined the NMR, structure of a 283-residue N-terminal fragment of immature HIV-1 Gag, (Gag(283)), which includes the intact matrix (MA) and N-terminal capsid, (CA(N)) domains. The beta-hairpin is unfolded in Gag(283), consistent with, the proposal that hairpin formation occurs subsequent to proteolytic, cleavage of Gag, triggering capsid assembly. Comparison of the immature, and mature CA(N) structures reveals that beta-hairpin formation induces a, approximately 2 A displacement of helix 6 and a concomitant displacement, of the cyclophylin-A (CypA)-binding loop, suggesting a possible allosteric, mechanism for CypA-mediated destabilization of the capsid particle during, infectivity.
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The capsid protein (CA) of the mature human immunodeficiency virus (HIV) contains an N-terminal beta-hairpin that is essential for formation of the capsid core particle. CA is generated by proteolytic cleavage of the Gag precursor polyprotein during viral maturation. We have determined the NMR structure of a 283-residue N-terminal fragment of immature HIV-1 Gag (Gag(283)), which includes the intact matrix (MA) and N-terminal capsid (CA(N)) domains. The beta-hairpin is unfolded in Gag(283), consistent with the proposal that hairpin formation occurs subsequent to proteolytic cleavage of Gag, triggering capsid assembly. Comparison of the immature and mature CA(N) structures reveals that beta-hairpin formation induces a approximately 2 A displacement of helix 6 and a concomitant displacement of the cyclophylin-A (CypA)-binding loop, suggesting a possible allosteric mechanism for CypA-mediated destabilization of the capsid particle during infectivity.
==About this Structure==
==About this Structure==
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1L6N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1L6N OCA].
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1L6N is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Human_immunodeficiency_virus_1 Human immunodeficiency virus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L6N OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Ndassa, Y.]]
[[Category: Ndassa, Y.]]
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[[Category: Summers, M.F.]]
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[[Category: Summers, M F.]]
[[Category: Tang, C.]]
[[Category: Tang, C.]]
[[Category: capsid]]
[[Category: capsid]]
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[[Category: maturation]]
[[Category: maturation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Thu Nov 8 14:16:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:42:00 2008''

Revision as of 11:42, 21 February 2008


1l6n

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STRUCTURE OF THE N-TERMINAL 283-RESIDUE FRAGMENT OF THE HIV-1 GAG POLYPROTEIN

Overview

The capsid protein (CA) of the mature human immunodeficiency virus (HIV) contains an N-terminal beta-hairpin that is essential for formation of the capsid core particle. CA is generated by proteolytic cleavage of the Gag precursor polyprotein during viral maturation. We have determined the NMR structure of a 283-residue N-terminal fragment of immature HIV-1 Gag (Gag(283)), which includes the intact matrix (MA) and N-terminal capsid (CA(N)) domains. The beta-hairpin is unfolded in Gag(283), consistent with the proposal that hairpin formation occurs subsequent to proteolytic cleavage of Gag, triggering capsid assembly. Comparison of the immature and mature CA(N) structures reveals that beta-hairpin formation induces a approximately 2 A displacement of helix 6 and a concomitant displacement of the cyclophylin-A (CypA)-binding loop, suggesting a possible allosteric mechanism for CypA-mediated destabilization of the capsid particle during infectivity.

About this Structure

1L6N is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

Structure of the N-terminal 283-residue fragment of the immature HIV-1 Gag polyprotein., Tang C, Ndassa Y, Summers MF, Nat Struct Biol. 2002 Jul;9(7):537-43. PMID:12032547

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