1jvk

<StructureSection load='1jvk' size='340' side='right' caption='[[1jvk]], [[Resolution|resolution]] 1.94&Aring;' scene=''>

<table><tr><td colspan='2'>[[1jvk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JVK FirstGlance]. <br>

</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1jvk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvk OCA], [http://pdbe.org/1jvk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jvk RCSB], [http://www.ebi.ac.uk/pdbsum/1jvk PDBsum]</span></td></tr>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jv/1jvk_consurf.spt"</scriptWhenChecked>

</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].

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== Publication Abstract from PubMed ==

The X-ray structure of an immunoglobulin light-chain dimer isolated from the urine as a "Bence-Jones protein" from a patient with multiple myeloma and amyloidosis (Sea) was determined at 1.94 A resolution and refined to R and R(free) factors of 0.22 and 0.25, respectively. This "amyloidogenic" protein crystallized in the orthorhombic P2(1)2(1)2(1) space group with unit-cell parameters a = 48.28, b = 83.32, c = 112.59 A as determined at 100 K. In the vital organs (heart and kidneys), the equivalent of the urinary protein produced fibrillar amyloid deposits which were fatal to the patient. Compared with the amyloidogenic Mcg light-chain dimer, the Sea protein was highly soluble in aqueous solutions and only crystallized at concentrations approaching 100 mg ml(-1). Both the Sea and Mcg proteins packed into crystals in highly ordered arrangements typical of strongly diffracting crystals of immunoglobulin fragments. Overall similarities and significant differences in the three-dimensional structures and crystalline properties are discussed for the Sea and Mcg Bence-Jones proteins, which together provide a generalized model of abnormalities present in lambda chains, facilitating a better understanding of amyloidosis of light-chain origin (AL).

Three-dimensional structure of an immunoglobulin light-chain dimer with amyloidogenic properties.,Bourne PC, Ramsland PA, Shan L, Fan ZC, DeWitt CR, Shultz BB, Terzyan SS, Moomaw CR, Slaughter CA, Guddat LW, Edmundson AB Acta Crystallogr D Biol Crystallogr. 2002 May;58(Pt 5):815-23. Epub 2002, Apr 26. PMID:11976493<ref>PMID:11976493</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1jvk" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bourne, P C]]

[[Category: DeWitt, C R]]

[[Category: Edmundson, A B]]

[[Category: Fan, Z C]]

[[Category: Ramsland, P A]]

[[Category: Shan, L]]

[[Category: Shultz, B B]]

[[Category: Terzyan, S S]]

[[Category: Immunoglobulin light chain dimer]]