1flh

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(New page: 200px<br /> <applet load="1flh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1flh, resolution 2.45&Aring;" /> '''CRYSTAL STRUCTURE O...)
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caption="1flh, resolution 2.45&Aring;" />
'''CRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTION'''<br />
'''CRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTION'''<br />
==Overview==
==Overview==
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The molecular structure of human uropepsin, an aspartic proteinase from, the urine produced in the form of pepsinogen A in the gastric mucosa, has, been determined by molecular replacement using human pepsin as the search, model. Crystals belong to space group P2(1)2(1)2(1), with unit-cell, parameters a = 50.99, b = 75.56, c = 89.90 A. Crystallographic refinement, led to an R factor of 0.161 at 2.45 A resolution. The positions of 2437, non-H protein atoms in 326 residues have been determined and the model, contains 143 water molecules. The structure is bilobal, consisting of two, predominantly beta-sheet lobes which, as observed in other aspartic, proteinases, are related by a pseudo-twofold axis. A model of the, uropepsin-pepstatin complex has been constructed based on the, high-resolution crystal structure of pepsin complexed with pepstatin.
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The molecular structure of human uropepsin, an aspartic proteinase from the urine produced in the form of pepsinogen A in the gastric mucosa, has been determined by molecular replacement using human pepsin as the search model. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.99, b = 75.56, c = 89.90 A. Crystallographic refinement led to an R factor of 0.161 at 2.45 A resolution. The positions of 2437 non-H protein atoms in 326 residues have been determined and the model contains 143 water molecules. The structure is bilobal, consisting of two predominantly beta-sheet lobes which, as observed in other aspartic proteinases, are related by a pseudo-twofold axis. A model of the uropepsin-pepstatin complex has been constructed based on the high-resolution crystal structure of pepsin complexed with pepstatin.
==About this Structure==
==About this Structure==
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1FLH 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/Pepsin_A Pepsin A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.1 3.4.23.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FLH OCA].
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1FLH 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/Pepsin_A Pepsin A], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.23.1 3.4.23.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FLH OCA].
==Reference==
==Reference==
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[[Category: Canduri, F.]]
[[Category: Canduri, F.]]
[[Category: Fadel, V.]]
[[Category: Fadel, V.]]
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[[Category: Gomes, R.A.S.]]
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[[Category: Gomes, R A.S.]]
[[Category: Hial, V.]]
[[Category: Hial, V.]]
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[[Category: Jr., W.F.De.Azevedo.]]
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[[Category: Jr., W F.De Azevedo.]]
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[[Category: Lorenzi, C.C.B.]]
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[[Category: Lorenzi, C C.B.]]
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[[Category: Neto, J.R.]]
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[[Category: Neto, J R.]]
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[[Category: Teodoro, L.G.V.L.]]
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[[Category: Teodoro, L G.V L.]]
[[Category: acid proteinase]]
[[Category: acid proteinase]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:39:56 2008''

Revision as of 10:40, 21 February 2008


1flh, resolution 2.45Å

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CRYSTAL STRUCTURE OF HUMAN UROPEPSIN AT 2.45 A RESOLUTION

Overview

The molecular structure of human uropepsin, an aspartic proteinase from the urine produced in the form of pepsinogen A in the gastric mucosa, has been determined by molecular replacement using human pepsin as the search model. Crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.99, b = 75.56, c = 89.90 A. Crystallographic refinement led to an R factor of 0.161 at 2.45 A resolution. The positions of 2437 non-H protein atoms in 326 residues have been determined and the model contains 143 water molecules. The structure is bilobal, consisting of two predominantly beta-sheet lobes which, as observed in other aspartic proteinases, are related by a pseudo-twofold axis. A model of the uropepsin-pepstatin complex has been constructed based on the high-resolution crystal structure of pepsin complexed with pepstatin.

About this Structure

1FLH is a Single protein structure of sequence from Homo sapiens. Active as Pepsin A, with EC number 3.4.23.1 Full crystallographic information is available from OCA.

Reference

Structure of human uropepsin at 2.45 A resolution., Canduri F, Teodoro LG, Fadel V, Lorenzi CC, Hial V, Gomes RA, Neto JR, de Azevedo WF Jr, Acta Crystallogr D Biol Crystallogr. 2001 Nov;57(Pt 11):1560-70. Epub 2001, Oct 25. PMID:11679720

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