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Open AccessJournal ArticleDOI

Atomic structure and chemistry of human serum albumin.

Xiao Min He, +1 more
- 16 Jul 1992 - 
- Vol. 358, Iss: 6383, pp 209-215
TLDR
The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 Å and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serumalbumin.
Abstract
The three-dimensional structure of human serum albumin has been determined crystallographically to a resolution of 2.8 A. It comprises three homologous domains that assemble to form a heart-shaped molecule. Each domain is a product of two subdomains that possess common structural motifs. The principal regions of ligand binding to human serum albumin are located in hydrophobic cavities in subdomains IIA and IIIA, which exhibit similar chemistry. The structure explains numerous physical phenomena and should provide insight into future pharmacokinetic and genetically engineered therapeutic applications of serum albumin.

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Citations
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Book ChapterDOI

Structure of serum albumin.

TL;DR: This chapter provides an insight of the findings of past significant papers with the current knowledge of the recently determined high resolution X-ray structure of serum albumin and suggests that AFP may have a higher affinity for some unknown ligands important for fetal development.
Journal ArticleDOI

A Novel Method for Measuring Antioxidant Capacity and its Application to Monitoring the Antioxidant Status in Premature Neonates

TL;DR: The method has been applied to investigate the total plasma antioxidant capacity of neonates and how this may be compromised in prematurity, and an antioxidant ranking was established based on their reactivity relative to a 1.0 mmol/l Trolox standard.
Journal ArticleDOI

Crystal structure of human serum albumin at 2.5 A resolution.

TL;DR: A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma or from a Pichia pastoris expression system, was obtained from polyethylene glycol 4000 solution, and three-dimensional structures of pHSA and rHSA were determined.
Journal ArticleDOI

Structural Basis of the Drug-Binding Specificity of Human Serum Albumin.

TL;DR: Crystallographic analysis of 17 different complexes of HSA with a wide variety of drugs and small-molecule toxins reveals the precise architecture of the two primary drug-binding sites on the protein, identifying residues that are key determinants of binding specificity and illuminating the capacity of both pockets for flexible accommodation.
Journal ArticleDOI

Delivery materials for siRNA therapeutics

TL;DR: An introduction to the biological challenges that siRNA delivery materials aim to overcome is provided, as well as a discussion of the way that the most effective and clinically advanced classes of si RNA delivery systems are designed to surmount these challenges.
References
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Journal ArticleDOI

Crystallographic R Factor Refinement by Molecular Dynamics

TL;DR: Test cases showed that the need for manual corrections during refinement of macromolecular crystal structures is reduced and the dynamics calculation moved residues that were misplaced by more than 3 angstroms into the correct positions without human intervention.
Book ChapterDOI

Resolution of phase ambiguity in macromolecular crystallography.

TL;DR: The method demonstrates a remarkable effectiveness for overcoming the phase ambiguity problem that has the major obstacle in the use of SIR or SAS data alone for macromolecular studies.
Journal ArticleDOI

The plasma proteins

Journal ArticleDOI

The detection of sub‐units within the crystallographic asymmetric unit

TL;DR: In this article, Rossmann and Blow describe how they have detected the existence of partial, approximate symmetry from a knowledge of the intensities alone, and the effect of noncrystallographic symmetry, whether partial or total, results in decreasing the size of the structure to be determined, while the number of observable intensities remains the same.
Journal ArticleDOI

The molecular replacement method

TL;DR: It is shown that the percentage of observed data and inaccuracy of the observed amplitudes available for phase extension are compensated by the extent of noncrystallographic redundancy and the fraction of crystal cell volume that may be flattened because it is outside the control of non Crystallographic symmetry.