3LU6

Human serum albumin in complex with compound 1

Summary for 3LU6

• Entry DOI: 10.2210/pdb3lu6/pdb
• Related: 3LU7 3LU8
• Descriptor: Serum albumin, [(1R,2R)-2-{[(5-fluoro-1H-indol-2-yl)carbonyl]amino}-2,3-dihydro-1H-inden-1-yl]acetic acid (3 entities in total)
• Functional Keywords: binding sites, ligands, protein binding, serum albumin, hsa, proteros biostructures gmbh, transport protein, astrazeneca, drug design
• Biological source: Homo sapiens (human)
• Cellular location: Secreted: P02768
• Total number of polymer chains: 2
• Total formula weight: 134551.87

Authors

Buttar, D.,Colclough, N.,Gerhardt, S.,MacFaul, P.A.,Phillips, S.D.,Plowright, A.,Whittamore, P.,Tam, K.,Maskos, K.,Steinbacher, S.,Steuber, H. (deposition date: 2010-02-17, release date: 2010-10-27, Last modification date: 2011-07-13)

Primary citation

Buttar, D.,Colclough, N.,Gerhardt, S.,Macfaul, P.A.,Phillips, S.D.,Plowright, A.,Whittamore, P.,Tam, K.,Maskos, K.,Steinbacher, S.,Steuber, H.
A combined spectroscopic and crystallographic approach to probing drug-human serum albumin interactions
Bioorg.Med.Chem., 18:7486-7496, 2010

PubMed Abstract: The displacement of probes that bind selectively to subdomains IIA or IIIA on human serum albumin (HSA) by competing compounds has been followed using fluorescence spectroscopy, and has therefore been used to assign a primary binding site for these compounds in the presence and absence of fatty acids. The crystal structures have also been solved for three compounds: a matched pair of carboxylic acids whose binding strength to HSA unexpectedly decreased as the lipophilicity increased; and a highly bound sulphonamide that appeared not to displace the probes in the displacement assay. The crystallography results support the findings from the fluorescence displacement assay. The results indicate that drug binding to subdomain IB might also be important location for certain compounds.

PubMed: 20869876
DOI: 10.1016/j.bmc.2010.08.052

Experimental method

X-RAY DIFFRACTION (2.7 Å)