1uhb

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(New page: 200px<br /><applet load="1uhb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uhb, resolution 2.15&Aring;" /> '''Crystal structure of...)
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[[Image:1uhb.jpg|left|200px]]<br /><applet load="1uhb" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1uhb.jpg|left|200px]]<br /><applet load="1uhb" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1uhb, resolution 2.15&Aring;" />
caption="1uhb, resolution 2.15&Aring;" />
'''Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution'''<br />
'''Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution'''<br />
==Overview==
==Overview==
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Trypsin, a serine protease enzyme plays a pivotal role in digestion and is, autocatalytic. The crystal structure of a complex formed between porcine, trypsin and an auto catalytically produced peptide is reported here. This, complex shows a reduction in enzyme activity as compared to native, beta-trypsin. The nonapeptide has a lysine, which is recognized by Asp 189, at the specificity pocket. The auto catalytically produced native, nonapeptide is bound at the active site cleft like other trypsin, inhibitors but the important interactions with the oxyanion hole are, absent. The peptide covers only a part of the active site cleft and hence, the enzyme activity is reduced rather than being inhibited.
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Trypsin, a serine protease enzyme plays a pivotal role in digestion and is autocatalytic. The crystal structure of a complex formed between porcine trypsin and an auto catalytically produced peptide is reported here. This complex shows a reduction in enzyme activity as compared to native beta-trypsin. The nonapeptide has a lysine, which is recognized by Asp 189 at the specificity pocket. The auto catalytically produced native nonapeptide is bound at the active site cleft like other trypsin inhibitors but the important interactions with the oxyanion hole are absent. The peptide covers only a part of the active site cleft and hence the enzyme activity is reduced rather than being inhibited.
==About this Structure==
==About this Structure==
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1UHB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with ACT and CA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1UHB OCA].
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1UHB is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa] with <scene name='pdbligand=ACT:'>ACT</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UHB OCA].
==Reference==
==Reference==
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[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
[[Category: Trypsin]]
[[Category: Trypsin]]
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[[Category: Ibrahim, B.Syed.]]
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[[Category: Ibrahim, B Syed.]]
[[Category: Pattabhi, V.]]
[[Category: Pattabhi, V.]]
[[Category: Shamaladevi, N.]]
[[Category: Shamaladevi, N.]]
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[[Category: serine protease]]
[[Category: serine protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:07:34 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:24:32 2008''

Revision as of 13:24, 21 February 2008


1uhb, resolution 2.15Å

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Crystal structure of porcine alpha trypsin bound with auto catalyticaly produced native peptide at 2.15 A resolution

Overview

Trypsin, a serine protease enzyme plays a pivotal role in digestion and is autocatalytic. The crystal structure of a complex formed between porcine trypsin and an auto catalytically produced peptide is reported here. This complex shows a reduction in enzyme activity as compared to native beta-trypsin. The nonapeptide has a lysine, which is recognized by Asp 189 at the specificity pocket. The auto catalytically produced native nonapeptide is bound at the active site cleft like other trypsin inhibitors but the important interactions with the oxyanion hole are absent. The peptide covers only a part of the active site cleft and hence the enzyme activity is reduced rather than being inhibited.

About this Structure

1UHB is a Protein complex structure of sequences from Sus scrofa with and as ligands. Active as Trypsin, with EC number 3.4.21.4 Full crystallographic information is available from OCA.

Reference

Trypsin activity reduced by an autocatalytically produced nonapeptide., Ibrahim BS, Shamaladevi N, Pattabhi V, J Biomol Struct Dyn. 2004 Jun;21(6):737-44. PMID:15106996

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