3bjl: Difference between revisions

Revision as of 18:50, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:3bjl.png

Template:STRUCTURE 3bjl

LOC, A LAMBDA 1 TYPE LIGHT-CHAIN DIMER (BENCE-JONES PROTEIN) CRYSTALLIZED IN AMMONIUM SULFATELOC, A LAMBDA 1 TYPE LIGHT-CHAIN DIMER (BENCE-JONES PROTEIN) CRYSTALLIZED IN AMMONIUM SULFATE

Template:ABSTRACT PUBMED 8692936

About this StructureAbout this Structure

3BJL is a Single protein structure of sequence from Homo sapiens. This structure supersedes the now removed PDB entry 1bjl. Full crystallographic information is available from OCA.

ReferenceReference

Three quaternary structures for a single protein., Huang DB, Ainsworth CF, Stevens FJ, Schiffer M, Proc Natl Acad Sci U S A. 1996 Jul 9;93(14):7017-21. PMID:8692936

Page seeded by OCA on Sun Jul 27 18:50:11 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''LOC, A LAMBDA 1 TYPE LIGHT-CHAIN DIMER (BENCE-JONES PROTEIN) CRYSTALLIZED IN AMMONIUM SULFATE'''
+===LOC, A LAMBDA 1 TYPE LIGHT-CHAIN DIMER (BENCE-JONES PROTEIN) CRYSTALLIZED IN AMMONIUM SULFATE===
-==Overview==
+<!--
-The structure of a multisubunit protein (immunoglobulin light chain) was solved in three crystal forms, differing only in the solvent of crystallization. The three structures were obtained at high ionic strength and low pH, high ionic strength and high pH, and low ionic strength and neutral pH. The three resulting "snapshots" of possible structures show that their variable-domain interactions differ, reflecting their stabilities under specific solvent conditions. In the three crystal forms, the variable domains had different rotational and translational relationships, whereas no alteration of the constant domains was found. The critical residues involved in the observed effect of the solvent are tryptophans and histidines located between the two variable domains in the dimeric structure. Tryptophan residues are commonly found in interfaces between proteins and their subunits, and histidines have been implicated in pH-dependent conformation changes. The quaternary structure observed for a multisubunit protein or protein complex in a crystal may be influenced by the interactions of the constituents within the molecule or complex and/or by crystal packing interactions. The comparison of buried surface areas and hydrogen bonds between the domains forming the molecule and between the molecules forming the crystals suggest that, for this system, the interactions within the molecule are most likely the determining factors.
+The line below this paragraph, {{ABSTRACT_PUBMED_8692936}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_8692936}}
 ==About this Structure==
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 [[Category: Bence jone]]
 [[Category: Multiple quaternary structure]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 20:51:14 2008''
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