This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

4nlj

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 11:16, 25 December 2014

Crystal structure of sheep beta-lactoglobulin (space group P1)

Structural highlights

4nlj is a 2 chain structure with sequence from Ovis aries. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	4nli
Resources:	FirstGlance, OCA, RCSB, PDBsum

Function

[LACB_SHEEP] Lactoglobulin is the primary component of whey, it binds retinol and is probably involved in the transport of that molecule.

Publication Abstract from PubMed

Ovine beta-lactoglobulin has been isolated from whey fraction of sheep milk and crystallized. The high-resolution structures of two crystal forms (triclinic and trigonal) obtained at pH 7.0 have been determined revealing that ovine protein, similarly to its bovine analog, is dimeric. Access to the binding site located in the eight-stranded antiparallel beta-barrel in both structures is blocked by the EF loop that has been found in closed conformation. Similarly to bovine lactoglobulin (BLG), conformation of the EF loop is stabilized by hydrogen bond between Glu89 and Ser116 indicating that Tanford transition might occur with the same mechanism. The substitution at six positions in relation to the most abundant isoform B of BLG also affects the distribution of electrostatic potentials and the total charge. (c) 2014 Wiley Periodicals, Inc. Biopolymers 101: 886-894, 2014.

Structure of two crystal forms of sheep beta-lactoglobulin with EF-loop in closed conformation.,Loch JI, Molenda M, Kopec M, Swiatek S, Lewinski K Biopolymers. 2014 Aug;101(8):886-94. doi: 10.1002/bip.22471. PMID:25098178^[1]

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

References

↑ Loch JI, Molenda M, Kopec M, Swiatek S, Lewinski K. Structure of two crystal forms of sheep beta-lactoglobulin with EF-loop in closed conformation. Biopolymers. 2014 Aug;101(8):886-94. doi: 10.1002/bip.22471. PMID:25098178 doi:http://dx.doi.org/10.1002/bip.22471

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/4nlj"

@@ Line 7: / Line 7: @@
 <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=4nlj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nlj OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4nlj RCSB], [http://www.ebi.ac.uk/pdbsum/4nlj PDBsum]</span></td></tr>
 </table>
+== Function ==
+[[http://www.uniprot.org/uniprot/LACB_SHEEP LACB_SHEEP]] Lactoglobulin is the primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

4nlj

From Proteopedia

Revision as of 11:16, 25 December 2014

Crystal structure of sheep beta-lactoglobulin (space group P1)

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox