1op2: Difference between revisions

Revision as of 11:49, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1op2.png

Template:STRUCTURE 1op2

Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutusCrystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus

Template:ABSTRACT PUBMED 15632114

About this StructureAbout this Structure

1OP2 is a Single protein structure of sequence from Deinagkistrodon acutus. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases., Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L, J Biol Chem. 2005 Mar 18;280(11):10524-9. Epub 2005 Jan 4. PMID:15632114

Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom., Zhu Z, Gong P, Teng M, Niu L, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):547-50. Epub 2003, Feb 21. PMID:12595722

Page seeded by OCA on Mon Jul 28 11:49:51 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1op2.gif|left|200px]]
+{{Seed}}
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 {{STRUCTURE_1op2|  PDB=1op2  |  SCENE=  }}
-'''Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus'''
+===Crystal Structure of AaV-SP-II, a Glycosylated Snake Venom Serine Proteinase from Agkistrodon acutus===
-==Overview==
+<!--
-We deduced that Agkistrodon actus venom serine proteinases I and II, previously isolated from the venom of A. acutus (Zhu, Z., Gong, P., Teng, M., and Niu, L. (2003) Acta Crystallogr. Sect. D Biol. Crystallogr. 59, 547-550), are encoded by two almost identical genes, with only the single substitution Asp for Asn at residue 62. Amidolytic assays indicated that they possess slightly different enzymatic properties. Crystal structures of A. actus venom serine proteinases I and II were determined at resolution of 2.0 and 2.1 A with the identification of trisaccharide (NAG(301)-FUC(302)-NAG(303)) and monosaccharide (NAG(301)) residues in them, respectively. The substrate binding sites S3 of the two proteinases appear much shallower than that of Trimeresurus stejnegeri venom plasminogen activator despite the overall structural similarity. Based on structural analysis, we showed that these Asn(35)-linked oligosaccharides collide spatially with some inhibitors, such as soybean trypsin inhibitor, and would therefore hinder their inhibitory binding. Difference of the carbohydrates in both the proteinases might also lead to their altered catalytic activities.
+The line below this paragraph, {{ABSTRACT_PUBMED_15632114}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15632114 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_15632114}}
 ==About this Structure==
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 ==Reference==
 Crystal structures and amidolytic activities of two glycosylated snake venom serine proteinases., Zhu Z, Liang Z, Zhang T, Zhu Z, Xu W, Teng M, Niu L, J Biol Chem. 2005 Mar 18;280(11):10524-9. Epub 2005 Jan 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/15632114 15632114]
+Purification, N-terminal sequencing, partial characterization, crystallization and preliminary crystallographic analysis of two glycosylated serine proteinases from Agkistrodon acutus venom., Zhu Z, Gong P, Teng M, Niu L, Acta Crystallogr D Biol Crystallogr. 2003 Mar;59(Pt 3):547-50. Epub 2003, Feb 21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12595722 12595722]
 [[Category: Deinagkistrodon acutus]]
 [[Category: Single protein]]
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 [[Category: Serine proteinase]]
 [[Category: Snake venom]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 04:06:57 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:49:51 2008''