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| - | [[Image:1lil.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1lil| PDB=1lil | SCENE= }} | | {{STRUCTURE_1lil| PDB=1lil | SCENE= }} |
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| - | '''BENCE JONES PROTEIN CLE, A LAMBDA III IMMUNOGLOBULIN LIGHT-CHAIN DIMER'''
| + | ===BENCE JONES PROTEIN CLE, A LAMBDA III IMMUNOGLOBULIN LIGHT-CHAIN DIMER=== |
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| - | ==Overview==
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| - | The structure of protein Cle, a human light-chain dimer from the lambdaIII subgroup, was determined using 2.6 A data; the R value is 18.4%. The structure was solved, after a false start, by molecular replacement with the lambdaII/V Mcg protein as a search structure. When the refinement did not proceed beyond an R value of 27%, it was discovered that while the constant domains were in their correct positions in the unit cell, the incorrect variable domains were used for defining the molecule. The correct solution required a rotation of 180 degrees around the local twofold axis that relates the two constant domains of the dimer. The correct variable domain positions overlap about 70% of the same volume as the incorrect ones of a symmetry-related molecule. The refinement distorted the geometries of the domains. Though the constant domains were in their correct positions, the r.m.s. (root-mean-square) deviation of the Calpha atom position was 1.2 A when the two constant domains were compared. For the correct structure, this value is 0.5 A. The phi and psi angles, the r.m.s. chiral value and the free R value, even when calculated a posteriori, were good indicators of the correctness of the structure. The quaternary structure of the Cle molecule is similar to that in Mcg (crystallized from ammonium sulfate); the elbow bend is 115 degrees. However, the arrangement of the variable domains differs from that observed in other variable domain dimers. The variable domains of Cle are 0.7 A closer than in Mcg or variable dimer Rei. The hydrogen bonding at the interface of the two domains is novel. Residues Tyr36 from both monomers form a hydrogen bond that is part of a network with the Gln89 residues from both monomers. For the first time hydrogen bonds were observed between the main-chain peptide N and O atoms of the complementarity-determining region CDR2 and CDR3 segments of both monomers. | + | The line below this paragraph, {{ABSTRACT_PUBMED_15299564}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15299564 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_15299564}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Bence jones protein]] | | [[Category: Bence jones protein]] |
| | [[Category: Immunoglobulin]] | | [[Category: Immunoglobulin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 23:57:24 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:59:08 2008'' |
Revision as of 17:59, 2 July 2008
Template:STRUCTURE 1lil
BENCE JONES PROTEIN CLE, A LAMBDA III IMMUNOGLOBULIN LIGHT-CHAIN DIMER
Template:ABSTRACT PUBMED 15299564
About this Structure
1LIL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Pitfalls of molecular replacement: the structure determination of an immunoglobulin light-chain dimer., Huang DB, Ainsworth C, Solomon A, Schiffer M, Acta Crystallogr D Biol Crystallogr. 1996 Nov 1;52(Pt 6):1058-66. PMID:15299564
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