Preliminary crystallographic analysis of a Fab specific for P-glycoprotein with and without bound peptide.J Mol Biol. 1994 Sep 02; 241(5):736-8.JM
Abstract
The antigen-binding fragment (Fab) of anti-peptide monoclonal antibody C219 raised against the multidrug resistance associated P-glycoprotein has been crystallized with and without bound peptide. The crystals of the Fab in the absence and presence of peptide belong to space groups P2(1) and P2(1)2(1)2(1), respectively. The volumes of both crystal forms are consistent with the presence of four Fab molecules per asymmetric unit. Diffraction data to 3.2 A resolution have been collected on a San Diego Multiwire Area Detector system from both crystal forms. Determination of the molecular replacement solutions is underway.
Links
MeSH
Pub Type(s)
Journal Article
Research Support, Non-U.S. Gov't
Language
eng
PubMed ID
7915332
Citation
Vasudevan, S, et al. "Preliminary Crystallographic Analysis of a Fab Specific for P-glycoprotein With and Without Bound Peptide." Journal of Molecular Biology, vol. 241, no. 5, 1994, pp. 736-8.
Vasudevan S, Johns KL, Rose DR. Preliminary crystallographic analysis of a Fab specific for P-glycoprotein with and without bound peptide. J Mol Biol. 1994;241(5):736-8.
Vasudevan, S., Johns, K. L., & Rose, D. R. (1994). Preliminary crystallographic analysis of a Fab specific for P-glycoprotein with and without bound peptide. Journal of Molecular Biology, 241(5), 736-8.
Vasudevan S, Johns KL, Rose DR. Preliminary Crystallographic Analysis of a Fab Specific for P-glycoprotein With and Without Bound Peptide. J Mol Biol. 1994 Sep 2;241(5):736-8. PubMed PMID: 7915332.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR
T1 - Preliminary crystallographic analysis of a Fab specific for P-glycoprotein with and without bound peptide.
AU - Vasudevan,S,
AU - Johns,K L,
AU - Rose,D R,
PY - 1994/9/2/pubmed
PY - 1994/9/2/medline
PY - 1994/9/2/entrez
SP - 736
EP - 8
JF - Journal of molecular biology
JO - J Mol Biol
VL - 241
IS - 5
N2 - The antigen-binding fragment (Fab) of anti-peptide monoclonal antibody C219 raised against the multidrug resistance associated P-glycoprotein has been crystallized with and without bound peptide. The crystals of the Fab in the absence and presence of peptide belong to space groups P2(1) and P2(1)2(1)2(1), respectively. The volumes of both crystal forms are consistent with the presence of four Fab molecules per asymmetric unit. Diffraction data to 3.2 A resolution have been collected on a San Diego Multiwire Area Detector system from both crystal forms. Determination of the molecular replacement solutions is underway.
SN - 0022-2836
UR - https://www.unboundmedicine.com/medline/citation/7915332/Preliminary_crystallographic_analysis_of_a_Fab_specific_for_P_glycoprotein_with_and_without_bound_peptide_
L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(84)71548-8
DB - PRIME
DP - Unbound Medicine
ER -