1awv: Difference between revisions

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[[Image:1awv.gif|left|200px]]<br />

[[Image:1awv.gif|left|200px]]<br /><applet load="1awv" size="350" color="white" frame="true" align="right" spinBox="true"

<applet load="1awv" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1awv, resolution 2.34Å" />

'''CYPA COMPLEXED WITH HVGPIA'''<br />

==Overview==

The cellular protein, cyclophilin A (CypA), is incorporated into the, virion of the type 1 human immunodeficiency virus (HIV-1) via a direct, interaction with the capsid domain of the viral Gag polyprotein. We, demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92, (87HAGPIA92) encompasses the primary cyclophilin A binding site and, present an X-ray crystal structure of the CypA/HAGPIA complex. In contrast, to the cis prolines observed in all previously reported structures of CypA, complexed with model peptides, the proline in this peptide, Pro 90, binds, the cyclophilin A active site in a trans conformation. We also report the, crystal structure of a complex between CypA and the hexapeptide HVGPIA, which also maintains the trans conformation. Comparison with the recently, determined structures of CypA in complexes with larger fragments of the, HIV-1 capsid protein demonstrates that CypA recognition of these, hexapeptides involves contacts with peptide residues Ala(Val) 88, Gly 89, and Pro 90, and is independent of the context of longer sequences.

The cellular protein, cyclophilin A (CypA), is incorporated into the virion of the type 1 human immunodeficiency virus (HIV-1) via a direct interaction with the capsid domain of the viral Gag polyprotein. We demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92 (87HAGPIA92) encompasses the primary cyclophilin A binding site and present an X-ray crystal structure of the CypA/HAGPIA complex. In contrast to the cis prolines observed in all previously reported structures of CypA complexed with model peptides, the proline in this peptide, Pro 90, binds the cyclophilin A active site in a trans conformation. We also report the crystal structure of a complex between CypA and the hexapeptide HVGPIA, which also maintains the trans conformation. Comparison with the recently determined structures of CypA in complexes with larger fragments of the HIV-1 capsid protein demonstrates that CypA recognition of these hexapeptides involves contacts with peptide residues Ala(Val) 88, Gly 89, and Pro 90, and is independent of the context of longer sequences.

==About this Structure==

1AWV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1AWV OCA].

1AWV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWV OCA].

==Reference==

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[[Category: Peptidylprolyl isomerase]]

[[Category: Single protein]]

[[Category: Vajdos, F.F.]]

[[Category: Vajdos, F F.]]

[[Category: complex (isomerase/peptide)]]

[[Category: cyclophilin a]]

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[[Category: pseudo-symmetry]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:04 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1awv.gif|left|200px]]<br />
+[[Image:1awv.gif|left|200px]]<br /><applet load="1awv" size="350" color="white" frame="true" align="right" spinBox="true"
-<applet load="1awv" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1awv, resolution 2.34&Aring;" />
 '''CYPA COMPLEXED WITH HVGPIA'''<br />
 ==Overview==
-The cellular protein, cyclophilin A (CypA), is incorporated into the, virion of the type 1 human immunodeficiency virus (HIV-1) via a direct, interaction with the capsid domain of the viral Gag polyprotein. We, demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92, (87HAGPIA92) encompasses the primary cyclophilin A binding site and, present an X-ray crystal structure of the CypA/HAGPIA complex. In contrast, to the cis prolines observed in all previously reported structures of CypA, complexed with model peptides, the proline in this peptide, Pro 90, binds, the cyclophilin A active site in a trans conformation. We also report the, crystal structure of a complex between CypA and the hexapeptide HVGPIA, which also maintains the trans conformation. Comparison with the recently, determined structures of CypA in complexes with larger fragments of the, HIV-1 capsid protein demonstrates that CypA recognition of these, hexapeptides involves contacts with peptide residues Ala(Val) 88, Gly 89, and Pro 90, and is independent of the context of longer sequences.
+The cellular protein, cyclophilin A (CypA), is incorporated into the virion of the type 1 human immunodeficiency virus (HIV-1) via a direct interaction with the capsid domain of the viral Gag polyprotein. We demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92 (87HAGPIA92) encompasses the primary cyclophilin A binding site and present an X-ray crystal structure of the CypA/HAGPIA complex. In contrast to the cis prolines observed in all previously reported structures of CypA complexed with model peptides, the proline in this peptide, Pro 90, binds the cyclophilin A active site in a trans conformation. We also report the crystal structure of a complex between CypA and the hexapeptide HVGPIA, which also maintains the trans conformation. Comparison with the recently determined structures of CypA in complexes with larger fragments of the HIV-1 capsid protein demonstrates that CypA recognition of these hexapeptides involves contacts with peptide residues Ala(Val) 88, Gly 89, and Pro 90, and is independent of the context of longer sequences.
 ==About this Structure==
-AWV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AWV OCA].
+AWV is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Active as [http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWV OCA].
 ==Reference==
@@ Line 15: / Line 14: @@
 [[Category: Peptidylprolyl isomerase]]
 [[Category: Single protein]]
-[[Category: Vajdos, F.F.]]
+[[Category: Vajdos, F F.]]
 [[Category: complex (isomerase/peptide)]]
 [[Category: cyclophilin a]]
@@ Line 21: / Line 20: @@
 [[Category: pseudo-symmetry]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:03:15 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:49:04 2008''