1l4v

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{{STRUCTURE_1l4v| PDB=1l4v | SCENE= }}
{{STRUCTURE_1l4v| PDB=1l4v | SCENE= }}
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'''SOLUTION STRUCTURE OF SAPECIN'''
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===SOLUTION STRUCTURE OF SAPECIN===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_2401368}}
==About this Structure==
==About this Structure==
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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].
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1L4V is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sarcophaga_peregrina Sarcophaga peregrina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4V OCA].
==Reference==
==Reference==
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[[Category: Takeuchi, K.]]
[[Category: Takeuchi, K.]]
[[Category: Antibacterial protein,insect defensin]]
[[Category: Antibacterial protein,insect defensin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:32:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 11:42:27 2008''

Revision as of 08:42, 2 July 2008

Template:STRUCTURE 1l4v

SOLUTION STRUCTURE OF SAPECIN

Template:ABSTRACT PUBMED 2401368

About this Structure

1L4V is a Single protein structure of sequence from Sarcophaga peregrina. Full experimental 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

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