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1pnb

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Revision as of 01:33, 10 September 2015

STRUCTURE OF NAPIN BNIB, NMR, 10 STRUCTURES

Structural highlights

1pnb is a 2 chain structure with sequence from Brassica napus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[2SSI_BRANA] The small, basic, water-soluble napins are one of the two major kinds of storage proteins synthesized in the seed during its maturation.

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

Napin BnIb is a representative member of the 2S albumin seed proteins, which consists of two polypeptide chains of 3.8 and 8.4 kDa linked by two disulfide bridges. In this work, a complete assignment of the 1H spectra of napin BnIb has been carried out by two-dimensional NMR sequence-specific methods and its secondary structure determined on the basis of spectral data. A calculation of the tertiary structure has been performed using approximately 500 distance constraints derived from unambiguously assigned NOE cross-correlations and distance geometry methods. The resulting global fold consists of five helices and a C-terminal loop arranged in a right-handed spiral. The folded protein is stabilized by two interchain disulfide bridges and two additional ones between cysteine residues in the large chain. The structure of napin BnIb represents a third example of a new and distinctive folding pattern first described for the hydrophobic protein from soybean and nonspecific lipid transfer proteins from wheat and maize. The presence of an internal cavity is not at all evident, which rules out in principle the napin BnIb as a carrier of lipids. The determined structure is compatible with activities attributed to these proteins such as phospholipid vesicle interaction, allergenicity, and calmodulin antagonism. Given the sequence homology of BnIb with other napins and napin-type 2S albumin seed proteins from different species, it is likely that all these proteins share a common architecture. The determined structure will be crucial to establish structure-function relationships and to explore the mechanisms of folding, processing, and deposition of these proteins. It will also provide a firm basis for a rational use of genetic engineering in order to develop improved transgenic plants.

1H NMR assignment and global fold of napin BnIb, a representative 2S albumin seed protein.,Rico M, Bruix M, Gonzalez C, Monsalve RI, Rodriguez R Biochemistry. 1996 Dec 10;35(49):15672-82. PMID:8961930^[1]

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

References

↑ Rico M, Bruix M, Gonzalez C, Monsalve RI, Rodriguez R. 1H NMR assignment and global fold of napin BnIb, a representative 2S albumin seed protein. Biochemistry. 1996 Dec 10;35(49):15672-82. PMID:8961930 doi:10.1021/bi961748q

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/1pnb"

@@ Line 3: / Line 3: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1pnb]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Brassica_napus Brassica napus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PNB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1PNB 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=1pnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pnb OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1pnb RCSB], [http://www.ebi.ac.uk/pdbsum/1pnb PDBsum]</span></td></tr>
+</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=1pnb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pnb OCA], [http://pdbe.org/1pnb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1pnb RCSB], [http://www.ebi.ac.uk/pdbsum/1pnb PDBsum]</span></td></tr>
 </table>
 == Function ==
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1pnb" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1pnb

From Proteopedia

Revision as of 01:33, 10 September 2015

STRUCTURE OF NAPIN BNIB, NMR, 10 STRUCTURES

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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