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| - | [[Image:1fyu.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1fyu| PDB=1fyu | SCENE= }} | | {{STRUCTURE_1fyu| PDB=1fyu | SCENE= }} |
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| - | '''Crystal structure of erythrina corallodendron lectin in hexagonal crystal form'''
| + | ===Crystal structure of erythrina corallodendron lectin in hexagonal crystal form=== |
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| - | ==Overview==
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| - | The Erythrina corallodendron lectin (EcorL) crystallizes in monoclinic and hexagonal crystal forms. Comparison of the newly determined hexagonal form (PDB code 1fyu) with the monoclinic form shows that the dimeric structure of EcorL reflects the inherent biological structure of the protein and is not an artifact of the crystal packing. To further understand the factors determining the dimerization modes of legume lectins, EcorL, concanavalin A (ConA), and Griffonia simplicifolia (GS4) were taken as representatives of the three unique dimers found in the family. Six virtual homodimers were generated. The hydropathy, amino acid composition, and solvation energy were calculated for all nine homodimers. Each of the three native dimers has a distinct chemical composition. EcorL has a dominant hydrophobic component, and ConA has a strong polar component, but in GS4 the three components contribute equally to the interface. This distribution pattern at the interface is unique to the native dimers and distinct from the partition observed in the virtual dimers. Amino acid composition of other members of the family that dimerize like EcorL or ConA maintain the same pattern of amino acids distribution observed in EcorL and ConA. However, lectins that dimerize like GS4 do not show a particularly distinct distribution. In all cases, the calculated solvation energy of the native dimer was lower than that of the virtual dimers, suggesting that the observed mode of dimerization is the most stable organization for the given sequence and tertiary structure. The dimerization type cannot be predicted by sequence analysis. | + | The line below this paragraph, {{ABSTRACT_PUBMED_11274466}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11274466 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11274466}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Lectin]] | | [[Category: Lectin]] |
| | [[Category: Protein-carbohydrate complex]] | | [[Category: Protein-carbohydrate complex]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:55:13 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:08:46 2008'' |
Revision as of 01:08, 1 July 2008
Template:STRUCTURE 1fyu
Crystal structure of erythrina corallodendron lectin in hexagonal crystal form
Template:ABSTRACT PUBMED 11274466
About this Structure
1FYU is a Single protein structure of sequence from Erythrina corallodendron. Full crystallographic information is available from OCA.
Reference
Chemical characteristics of dimer interfaces in the legume lectin family., Elgavish S, Shaanan B, Protein Sci. 2001 Apr;10(4):753-61. PMID:11274466
Page seeded by OCA on Tue Jul 1 04:08:46 2008
