1m93

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(New page: 200px<br /><applet load="1m93" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m93, resolution 1.65&Aring;" /> '''1.65 A Structure of ...)
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caption="1m93, resolution 1.65&Aring;" />
'''1.65 A Structure of Cleaved Viral Serpin CRMA'''<br />
'''1.65 A Structure of Cleaved Viral Serpin CRMA'''<br />
==Overview==
==Overview==
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CrmA is an unusual viral serpin that inhibits both cysteine and serine, proteinases involved in the regulation of host inflammatory and apoptosis, processes. It differs from other members of the serpin superfamily by, having a reactive center loop that is one residue shorter, and by its, apparent inability to form SDS-stable covalent complexes with cysteine, proteinases. To obtain insight into the inhibitory mechanism of crmA, we, determined the crystal structure of reactive center loop-cleaved crmA to, 2.9 A resolution. The structure, which is the first of a viral serpin, suggests that crmA can inhibit cysteine proteinases by a mechanism, analogous to that used by other serpins against serine proteinases., However, one striking difference from other serpins, which may be, significant for in vivo function, is an additional highly charged, antiparallel strand for b sheet A, whose sequence and length are unique to, crmA.
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CrmA is an unusual viral serpin that inhibits both cysteine and serine proteinases involved in the regulation of host inflammatory and apoptosis processes. It differs from other members of the serpin superfamily by having a reactive center loop that is one residue shorter, and by its apparent inability to form SDS-stable covalent complexes with cysteine proteinases. To obtain insight into the inhibitory mechanism of crmA, we determined the crystal structure of reactive center loop-cleaved crmA to 2.9 A resolution. The structure, which is the first of a viral serpin, suggests that crmA can inhibit cysteine proteinases by a mechanism analogous to that used by other serpins against serine proteinases. However, one striking difference from other serpins, which may be significant for in vivo function, is an additional highly charged antiparallel strand for b sheet A, whose sequence and length are unique to crmA.
==About this Structure==
==About this Structure==
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1M93 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cupixi_virus Cupixi virus] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M93 OCA].
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1M93 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Cupixi_virus Cupixi virus] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M93 OCA].
==Reference==
==Reference==
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[[Category: Cupixi virus]]
[[Category: Cupixi virus]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Gettins, P.G.W.]]
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[[Category: Gettins, P G.W.]]
[[Category: Simonovic, M.]]
[[Category: Simonovic, M.]]
[[Category: Volz, K.]]
[[Category: Volz, K.]]
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[[Category: serpin]]
[[Category: serpin]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:14:54 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:46 2008''

Revision as of 11:52, 21 February 2008

Image:1m93.gif

1m93, resolution 1.65Å

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1.65 A Structure of Cleaved Viral Serpin CRMA

Overview

CrmA is an unusual viral serpin that inhibits both cysteine and serine proteinases involved in the regulation of host inflammatory and apoptosis processes. It differs from other members of the serpin superfamily by having a reactive center loop that is one residue shorter, and by its apparent inability to form SDS-stable covalent complexes with cysteine proteinases. To obtain insight into the inhibitory mechanism of crmA, we determined the crystal structure of reactive center loop-cleaved crmA to 2.9 A resolution. The structure, which is the first of a viral serpin, suggests that crmA can inhibit cysteine proteinases by a mechanism analogous to that used by other serpins against serine proteinases. However, one striking difference from other serpins, which may be significant for in vivo function, is an additional highly charged antiparallel strand for b sheet A, whose sequence and length are unique to crmA.

About this Structure

1M93 is a Protein complex structure of sequences from Cupixi virus with as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of viral serpin crmA provides insights into its mechanism of cysteine proteinase inhibition., Simonovic M, Gettins PGW, Volz K, Protein Sci. 2000 Aug;9(8):1423-7. PMID:10975564

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