1l4v
From Proteopedia
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| - | [[Image:1l4v.gif|left|200px]] | + | [[Image:1l4v.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF SAPECIN''' | + | {{Structure |
| + | |PDB= 1l4v |SIZE=350|CAPTION= <scene name='initialview01'>1l4v</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF SAPECIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1L4V is a [ | + | 1L4V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sarcophaga_peregrina Sarcophaga peregrina]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4V OCA]. |
==Reference== | ==Reference== | ||
| - | 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin., Hanzawa H, Shimada I, Kuzuhara T, Komano H, Kohda D, Inagaki F, Natori S, Arata Y, FEBS Lett. 1990 Sep 3;269(2):413-20. PMID:[http:// | + | 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin., Hanzawa H, Shimada I, Kuzuhara T, Komano H, Kohda D, Inagaki F, Natori S, Arata Y, FEBS Lett. 1990 Sep 3;269(2):413-20. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2401368 2401368] |
[[Category: Sarcophaga peregrina]] | [[Category: Sarcophaga peregrina]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: insect defensin]] | [[Category: insect defensin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:26:20 2008'' |
Revision as of 10:26, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF SAPECIN
Overview
The solution conformation of an antibacterial protein sapecin has been determined by 1H nuclear magnetic resonance (NMR) and dynamical simulated annealing calculations. It has been shown that the polypeptide fold consists of one flexible loop (residues 4-12), one helix (residues 15-23), and two extended strands (residues 24-31 and 34-40). It was found that the tertiary structure of sapecin is completely different from that of rabbit neutrophil defensin NP-5, which is homologous to sapecin in the amino acid sequences and also has the antibacterial activity. The three-dimensional structure determination has revealed that a basic-residue rich region and the hydrophobic surface face each other on the surface of sapecin.
About this Structure
1L4V is a Single protein structure of sequence from Sarcophaga peregrina. Full crystallographic information is available from OCA.
Reference
1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin., Hanzawa H, Shimada I, Kuzuhara T, Komano H, Kohda D, Inagaki F, Natori S, Arata Y, FEBS Lett. 1990 Sep 3;269(2):413-20. PMID:2401368
Page seeded by OCA on Thu Mar 20 12:26:20 2008
