Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

2XVQ

Human serum albumin complexed with dansyl-L-sarcosine

Summary for 2XVQ
Entry DOI10.2210/pdb2xvq/pdb
Related1AO6 1BJ5 1BKE 1BM0 1E78 1E7A 1E7B 1E7C 1E7E 1E7F 1E7G 1E7H 1E7I 1GNI 1GNJ 1H9Z 1HA2 1HK1 1HK2 1HK3 1HK4 1HK5 1N5U 1O9X 1TF0 1UOR 1YSX 2BX8 2BXA 2BXB 2BXC 2BXD 2BXE 2BXF 2BXG 2BXH 2BXI 2BXK 2BXL 2BXM 2BXN 2BXO 2BXP 2BXQ 2ESG 2VDB 2VUE 2VUF 2XSI 2XVU 2XVV 2XVW 2XW0 2XW1
DescriptorSERUM ALBUMIN, DANSYL-L-SARCOSINE (2 entities in total)
Functional Keywordstransport protein
Biological sourceHOMO SAPIENS (HUMAN)
Total number of polymer chains2
Total formula weight133787.20
Authors
Ryan, A.J.,Curry, S. (deposition date: 2010-10-27, release date: 2010-11-10, Last modification date: 2024-10-23)
Primary citationRyan, A.J.,Ghuman, J.,Zunszain, P.A.,Chung, C.W.,Curry, S.
Structural Basis of Binding of Fluorescent, Site-Specific Dansylated Amino Acids to Human Serum Albumin.
J.Struct.Biol., 174:84-, 2011
Cited by
PubMed Abstract: Human serum albumin (HSA) has two primary binding sites for drug molecules. These sites selectively bind different dansylated amino acid compounds, which-due to their intrinsic fluorescence-have long been used as specific markers for the drug pockets on HSA. We present here the co-crystal structures of HSA in complex with six dansylated amino acids that are specific for either drug site 1 (dansyl-l-asparagine, dansyl-l-arginine, dansyl-l-glutamate) or drug site 2 (dansyl-l-norvaline, dansyl-l-phenylalanine, dansyl-l-sarcosine). Our results explain the structural basis of the site-specificity of different dansylated amino acids. They also show that fatty acid binding has only a modest effect on binding of dansylated amino acids to drug site 1 and identify the location of secondary binding sites.
PubMed: 20940056
DOI: 10.1016/J.JSB.2010.10.004
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

229183

PDB entries from 2024-12-18

PDB statisticsPDBj update infoContact PDBjnumon