2gnm

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{{STRUCTURE_2gnm| PDB=2gnm | SCENE= }}
{{STRUCTURE_2gnm| PDB=2gnm | SCENE= }}
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'''P. angolensis lectin (PAL) treated with EDTA for 39 hours'''
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===P. angolensis lectin (PAL) treated with EDTA for 39 hours===
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==Overview==
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The interplay between metal binding, carbohydrate binding activity, stability and structure of the lectin from Pterocarpus angolensis was investigated. Removal of the metals leads to a more flexible form of the protein with significantly less conformational stability. Crystal structures of this metal-free form show significant structural rearrangements, although some structural features that allow the binding of sugars are retained. We propose that substitution of an asparagine residue at the start of the C-terminal beta-strand of the legume lectin monomer hinders the trans-isomerization of the cis-peptide bond upon demetallization and constitutes an intramolecular switch governing the isomer state of the non-proline bond and ultimately the lectin phenotype.
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(as it appears on PubMed at http://www.pubmed.gov), where 16824540 is the PubMed ID number.
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{{ABSTRACT_PUBMED_16824540}}
==About this Structure==
==About this Structure==
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[[Category: Pal]]
[[Category: Pal]]
[[Category: Sugar complex]]
[[Category: Sugar complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:19:12 2008''

Revision as of 14:19, 28 July 2008

Image:2gnm.png

Template:STRUCTURE 2gnm

P. angolensis lectin (PAL) treated with EDTA for 39 hours

Template:ABSTRACT PUBMED 16824540

About this Structure

2GNM is a Single protein structure of sequence from Pterocarpus angolensis. Full crystallographic information is available from OCA.

Reference

Interplay between metal binding and cis/trans isomerization in legume lectins: structural and thermodynamic study of P. angolensis lectin., Garcia-Pino A, Buts L, Wyns L, Loris R, J Mol Biol. 2006 Aug 4;361(1):153-67. Epub 2006 Jun 21. PMID:16824540

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