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| - | [[Image:1pc8.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1pc8| PDB=1pc8 | SCENE= }} | | {{STRUCTURE_1pc8| PDB=1pc8 | SCENE= }} |
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| - | '''Crystal Structure of a novel form of mistletoe lectin from Himalayan Viscum album L. at 3.8A resolution'''
| + | ===Crystal Structure of a novel form of mistletoe lectin from Himalayan Viscum album L. at 3.8A resolution=== |
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| - | ==Overview==
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| - | This is the first report of the structural studies of a novel ribosome-inactivating protein (RIP) obtained from the Himalayan mistletoe (Viscum album) (HmRip). HmRip is a type II heterodimeric protein consisting of a toxic enzyme (A-chain) with an active site for ribosome inactivation and a lectin subunit (B-chain) with well defined sugar-binding sites. The crystal structure of HmRip has been determined at 3.8 A resolution and refined to a crystallographic R factor of 0.228 (R(free) = 0.271). A comparison of this structure with other type II RIPs reveals the presence of distinct structural features in the active site of the A-chain and in the 2gamma sugar-binding site of the B-chain. The conformation of the side chain of Tyr110, which is a conserved active-site residue in the A subunit, is strikingly different from those observed in other mistletoe RIPs, indicating its unique substrate-binding preference. The deletion of two important residues from the kink region after Ala231 in the 2gamma subdomain of the B-chain results in a significantly different conformation of the sugar-binding pocket. A ribosome-recognition site has also been identified in HmRip. The site is a shallow cavity, with the conserved residues Arg51, Asp70, Thr72 and Asn73 involved in the binding. The conformations of the antigenic epitopes of residues 1-20, 85-103 and 206-223 differ from those observed in other type II RIPs, resulting in the distinct antigenicity and pharmacological properties of HmRip.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15583377}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15583377 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15583377}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Mistletoe lectin]] | | [[Category: Mistletoe lectin]] |
| | [[Category: Novel form]] | | [[Category: Novel form]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:55:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 12:25:10 2008'' |
Revision as of 09:25, 27 July 2008
Template:STRUCTURE 1pc8
Crystal Structure of a novel form of mistletoe lectin from Himalayan Viscum album L. at 3.8A resolution
Template:ABSTRACT PUBMED 15583377
About this Structure
1PC8 is a Protein complex structure of sequences from Viscum album. Full crystallographic information is available from OCA.
Reference
Structure of a novel ribosome-inactivating protein from a hemi-parasitic plant inhabiting the northwestern Himalayas., Mishra V, Ethayathulla AS, Sharma RS, Yadav S, Krauspenhaar R, Betzel C, Babu CR, Singh TP, Acta Crystallogr D Biol Crystallogr. 2004 Dec;60(Pt 12 Pt 2):2295-304., Epub 2004 Nov 26. PMID:15583377
Page seeded by OCA on Sun Jul 27 12:25:10 2008
