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1l4v

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Revision as of 05:52, 28 April 2021

SOLUTION STRUCTURE OF SAPECIN

Structural highlights

1l4v is a 1 chain structure with sequence from Boettcherisca peregrina. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SAPE_SARPE] Sapecins, which are potent bactericidal proteins, are produced in response to injury. Sapecin is cytotoxic to Gram-positive bacteria, and to a lesser extent against Gram-negative bacteria.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hanzawa H, Shimada I, Kuzuhara T, Komano H, Kohda D, Inagaki F, Natori S, Arata Y. 1H nuclear magnetic resonance study of the solution conformation of an antibacterial protein, sapecin. FEBS Lett. 1990 Sep 3;269(2):413-20. PMID:2401368

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1l4v"

@@ Line 3: / Line 3: @@
 <StructureSection load='1l4v' size='340' side='right'caption='[[1l4v]], [[NMR_Ensembles_of_Models | 18 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1l4v]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Boettcherisca_peregrina Boettcherisca peregrina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4V OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1L4V FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1l4v]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Boettcherisca_peregrina Boettcherisca peregrina]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1L4V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1L4V FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1l4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4v OCA], [http://pdbe.org/1l4v PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1l4v RCSB], [http://www.ebi.ac.uk/pdbsum/1l4v PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4v ProSAT]</span></td></tr>
+</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1l4v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1l4v OCA], [https://pdbe.org/1l4v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1l4v RCSB], [https://www.ebi.ac.uk/pdbsum/1l4v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1l4v ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/SAPE_SARPE SAPE_SARPE]] Sapecins, which are potent bactericidal proteins, are produced in response to injury. Sapecin is cytotoxic to Gram-positive bacteria, and to a lesser extent against Gram-negative bacteria.
+[[https://www.uniprot.org/uniprot/SAPE_SARPE SAPE_SARPE]] Sapecins, which are potent bactericidal proteins, are produced in response to injury. Sapecin is cytotoxic to Gram-positive bacteria, and to a lesser extent against Gram-negative bacteria.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1l4v

From Proteopedia

Revision as of 05:52, 28 April 2021

SOLUTION STRUCTURE OF SAPECIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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