| pubmed-article:8568901 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8568901 | lifeskim:mentions | umls-concept:C0003242 | lld:lifeskim |
| pubmed-article:8568901 | lifeskim:mentions | umls-concept:C0444626 | lld:lifeskim |
| pubmed-article:8568901 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:8568901 | pubmed:dateCreated | 1996-3-7 | lld:pubmed |
| pubmed-article:8568901 | pubmed:abstractText | The structure of the Fab fragment of the mouse anti-anti-idiotypic monoclonal antibody (mAb) GH1002 was solved by X-ray crystallography. mAb GH1002 was elicited with the syngeneic anti-idiotype mAb MK2-23 which mimics the determinant defined by anti-human high molecular weight-melanoma associated antigen (HMW-MAA) mAb 763.74. The Fab fragments of mAb GH1002 exist in the crystal as dimers related by crystallographic 2-fold axes. The interface between dyad-related Fab fragments is formed primarily by interaction of the hypervariable loops of one with the other. The self-interaction of Fab fragments of anti-anti-idiotypic mAb GH1002 through their combining sites is extremely tight and intricate, closely resembling that observed in structures of id-anti-id complexes, and comparable in terms of total contact area, charge complementarity, and number of hydrogen bonds. The self-complementarity of the antibody observed here could be coincidental and thus reflect some non-specific binding capability. It might, on the other hand, be immunologically relevant and exemplify a certain degree of evolved self complementarity characteristic of antibodies participating in idiotypic cascades. | lld:pubmed |
| pubmed-article:8568901 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8568901 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8568901 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8568901 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8568901 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8568901 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8568901 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8568901 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8568901 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8568901 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8568901 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:8568901 | pubmed:issn | 0022-2836 | lld:pubmed |
| pubmed-article:8568901 | pubmed:author | pubmed-author:FerroneSS | lld:pubmed |
| pubmed-article:8568901 | pubmed:author | pubmed-author:BarRR | lld:pubmed |
| pubmed-article:8568901 | pubmed:author | pubmed-author:McPhersonAA | lld:pubmed |
| pubmed-article:8568901 | pubmed:author | pubmed-author:DayJJ | lld:pubmed |
| pubmed-article:8568901 | pubmed:author | pubmed-author:WangXX | lld:pubmed |
| pubmed-article:8568901 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8568901 | pubmed:day | 2 | lld:pubmed |
| pubmed-article:8568901 | pubmed:volume | 255 | lld:pubmed |
| pubmed-article:8568901 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8568901 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8568901 | pubmed:pagination | 617-27 | lld:pubmed |
| pubmed-article:8568901 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:meshHeading | pubmed-meshheading:8568901-... | lld:pubmed |
| pubmed-article:8568901 | pubmed:year | 1996 | lld:pubmed |
| pubmed-article:8568901 | pubmed:articleTitle | Crystal structure of an anti-anti-idiotype shows it to be self-complementary. | lld:pubmed |
| pubmed-article:8568901 | pubmed:affiliation | Department of Biochemistry, University of California at Riverside 92521, USA. | lld:pubmed |
| pubmed-article:8568901 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8568901 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8568901 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
