2ptl: Difference between revisions

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[[Image:2ptl.jpg|left|200px]]
{{Seed}}
[[Image:2ptl.png|left|200px]]


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{{STRUCTURE_2ptl|  PDB=2ptl  |  SCENE=  }}  
{{STRUCTURE_2ptl|  PDB=2ptl  |  SCENE=  }}  


'''THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN IMMUNOGLOBULIN LIGHT CHAIN-BINDING DOMAIN OF PROTEIN L. COMPARISON WITH THE IGG-BINDING DOMAINS OF PROTEIN G'''
===THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN IMMUNOGLOBULIN LIGHT CHAIN-BINDING DOMAIN OF PROTEIN L. COMPARISON WITH THE IGG-BINDING DOMAINS OF PROTEIN G===




==Overview==
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Protein L is a multidomain protein expressed at the surface of some strains of the anaerobic bacterial species Peptostreptococcus magnus. It has affinity for immunoglobulin (Ig) through interaction with framework structures in the variable Ig light chain domain. The Ig-binding activity is located to five homologous repeats called B1-B5 in the N-terminal part of the protein. We have determined the three-dimensional solution structure of the 76 amino acid residue long B1 domain using NMR spectroscopy and distance geometry-restrained simulated annealing. The domain is composed of a 15 amino acid residue long disordered N-terminus followed by a folded portion comprising an alpha-helix packed against a four-stranded beta-sheet. These secondary structural elements are well determined with a backbone atomic root mean square deviation from their mean of 0.54 A. The B domains of protein L show very limited sequence homology to the domains of streptococcal protein G interacting with the heavy chains of IgG. However, despite this fact, and their different binding properties, the fold of the B1 domain was found to be similar to the fold of the IgG-binding protein G domains [Wikstrom, M., Sjobring, U., Kastern, W., Bjorck, L., Drakenberg, T., &amp; Forsen, S. (1993) Biochemistry 32, 3381-3386]. In the present study, the solution structure of the B1 domain enabled a more detailed comparison which can explain the different Ig-binding specificities of these two bacterial surface proteins. Among the differences observed, the alpha-helix orientation is the most striking.(ABSTRACT TRUNCATED AT 250 WORDS)
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{{ABSTRACT_PUBMED_7947810}}


==About this Structure==
==About this Structure==
2PTL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTL OCA].  
2PTL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Finegoldia_magna Finegoldia magna]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PTL OCA].  


==Reference==
==Reference==
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[[Category: Sjoebring, U.]]
[[Category: Sjoebring, U.]]
[[Category: Wikstroem, M.]]
[[Category: Wikstroem, M.]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 13:47:04 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 10:12:38 2008''

Revision as of 07:12, 28 July 2008

File:2ptl.png

Template:STRUCTURE 2ptl

THREE-DIMENSIONAL SOLUTION STRUCTURE OF AN IMMUNOGLOBULIN LIGHT CHAIN-BINDING DOMAIN OF PROTEIN L. COMPARISON WITH THE IGG-BINDING DOMAINS OF PROTEIN G

Template:ABSTRACT PUBMED 7947810

About this Structure

2PTL is a Single protein structure of sequence from Finegoldia magna. Full experimental information is available from OCA.

Reference

Three-dimensional solution structure of an immunoglobulin light chain-binding domain of protein L. Comparison with the IgG-binding domains of protein G., Wikstrom M, Drakenberg T, Forsen S, Sjobring U, Bjorck L, Biochemistry. 1994 Nov 29;33(47):14011-7. PMID:7947810

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