2pel
From Proteopedia
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[[Image:2pel.jpg|left|200px]] | [[Image:2pel.jpg|left|200px]] | ||
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'''PEANUT LECTIN''' | '''PEANUT LECTIN''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2PEL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. This structure supersedes the now removed PDB entry | + | 2PEL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Arachis_hypogaea Arachis hypogaea]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1pel 1pel]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PEL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Surolia, A.]] | [[Category: Surolia, A.]] | ||
[[Category: Vijayan, M.]] | [[Category: Vijayan, M.]] | ||
| - | [[Category: | + | [[Category: Agglutinin]] |
| - | [[Category: | + | [[Category: Carbohydrate specificity]] |
| - | [[Category: | + | [[Category: Legume lectin]] |
| - | [[Category: | + | [[Category: Open quaternary structure]] |
| - | [[Category: | + | [[Category: Protein crystallography]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 12:58:14 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 09:58, 4 May 2008
PEANUT LECTIN
Overview
The structure of the complex of the tetrameric peanut lectin with lactose has been refined to an R-value of 16.4% using 2.25 angstroms resolution X-ray diffraction data. The subunit conformation in the structure is similar to that in other legume lectins except in the loops. It has been shown that in the tertiary structure of legume lectins, the short five-stranded sheet plays a major role in connecting the larger flat six-stranded and curved seven-stranded sheets. Furthermore, the loops that connect the strands at the two ends of the seven-stranded sheet curve toward and interact with each other to produce a second hydrophobic core in addition to the one between the two large sheets. The protein-lactose interactions involve the invariant features observed in other legume lectins in addition to those characteristic of peanut lectin. The "open" quaternary association in peanut lectin is stabilised by hydrophobic, hydrogen-bonded and water-mediated interactions. Contrary to the earlier belief, the structure of peanut lectin demonstrates that the variability in quaternary association in legume lectins, despite all of them having nearly the same tertiary structure, is not necessarily caused by covalently bound carbohydrate. An attempt has been made to provide a structural rationale for this variability, on the basis of buried surface areas during dimerisation. A total of 45 water molecules remain invariant when the hydration shells of the four subunits are compared. A majority of them appear to be involved in stabilising loops.
About this Structure
2PEL is a Single protein structure of sequence from Arachis hypogaea. This structure supersedes the now removed PDB entry 1pel. Full crystallographic information is available from OCA.
Reference
Conformation, protein-carbohydrate interactions and a novel subunit association in the refined structure of peanut lectin-lactose complex., Banerjee R, Das K, Ravishankar R, Suguna K, Surolia A, Vijayan M, J Mol Biol. 1996 Jun 7;259(2):281-96. PMID:8656429 Page seeded by OCA on Sun May 4 12:58:14 2008
