1bm0

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(New page: 200px<br /> <applet load="1bm0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bm0, resolution 2.50&Aring;" /> '''CRYSTAL STRUCTURE O...)
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'''CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN'''<br />
'''CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN'''<br />
==Overview==
==Overview==
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A new triclinic crystal form of human serum albumin (HSA), derived either, from pool plasma (pHSA) or from a Pichia pastoris expression system, (rHSA), was obtained from polyethylene glycol 4000 solution., Three-dimensional structures of pHSA and rHSA were determined at 2.5 A, resolution from the new triclinic crystal form by molecular replacement, using atomic coordinates derived from a multiple isomorphous replacement, work with a known tetragonal crystal form. The structures of pHSA and rHSA, are virtually identical, with an r.m. s. deviation of 0.24 A for all, Calpha atoms. The two HSA molecules involved in the asymmetric unit are, related by a strict local twofold symmetry such that the Calpha atoms of, the two molecules can be superimposed with an r.m.s. deviation of 0.28 A, in pHSA. Cys34 is the only cysteine with a free sulfhydryl group which, does not participate in a disulfide linkage with any external ligand., Domains II and III both have a pocket formed mostly of hydrophobic and, positively charged residues and in which a very wide range of compounds, may be accommodated. Three tentative binding sites for long-chain fatty, acids, each with different surroundings, are located at the surface of, each domain.
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A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma (pHSA) or from a Pichia pastoris expression system (rHSA), was obtained from polyethylene glycol 4000 solution. Three-dimensional structures of pHSA and rHSA were determined at 2.5 A resolution from the new triclinic crystal form by molecular replacement, using atomic coordinates derived from a multiple isomorphous replacement work with a known tetragonal crystal form. The structures of pHSA and rHSA are virtually identical, with an r.m. s. deviation of 0.24 A for all Calpha atoms. The two HSA molecules involved in the asymmetric unit are related by a strict local twofold symmetry such that the Calpha atoms of the two molecules can be superimposed with an r.m.s. deviation of 0.28 A in pHSA. Cys34 is the only cysteine with a free sulfhydryl group which does not participate in a disulfide linkage with any external ligand. Domains II and III both have a pocket formed mostly of hydrophobic and positively charged residues and in which a very wide range of compounds may be accommodated. Three tentative binding sites for long-chain fatty acids, each with different surroundings, are located at the surface of each domain.
==Disease==
==Disease==
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==About this Structure==
==About this Structure==
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1BM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BM0 OCA].
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1BM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BM0 OCA].
==Reference==
==Reference==
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[[Category: carrier protein]]
[[Category: carrier protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:11:35 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:56:40 2008''

Revision as of 09:56, 21 February 2008


1bm0, resolution 2.50Å

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CRYSTAL STRUCTURE OF HUMAN SERUM ALBUMIN

Contents

Overview

A new triclinic crystal form of human serum albumin (HSA), derived either from pool plasma (pHSA) or from a Pichia pastoris expression system (rHSA), was obtained from polyethylene glycol 4000 solution. Three-dimensional structures of pHSA and rHSA were determined at 2.5 A resolution from the new triclinic crystal form by molecular replacement, using atomic coordinates derived from a multiple isomorphous replacement work with a known tetragonal crystal form. The structures of pHSA and rHSA are virtually identical, with an r.m. s. deviation of 0.24 A for all Calpha atoms. The two HSA molecules involved in the asymmetric unit are related by a strict local twofold symmetry such that the Calpha atoms of the two molecules can be superimposed with an r.m.s. deviation of 0.28 A in pHSA. Cys34 is the only cysteine with a free sulfhydryl group which does not participate in a disulfide linkage with any external ligand. Domains II and III both have a pocket formed mostly of hydrophobic and positively charged residues and in which a very wide range of compounds may be accommodated. Three tentative binding sites for long-chain fatty acids, each with different surroundings, are located at the surface of each domain.

Disease

Known diseases associated with this structure: Analbuminemia OMIM:[103600], Dysalbuminemic hyperthyroxinemia OMIM:[103600], Dysalbuminemic hyperzincemia OMIM:[103600]

About this Structure

1BM0 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human serum albumin at 2.5 A resolution., Sugio S, Kashima A, Mochizuki S, Noda M, Kobayashi K, Protein Eng. 1999 Jun;12(6):439-46. PMID:10388840

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