1hbs
From Proteopedia
| Line 1: | Line 1: | ||
| - | [[Image:1hbs. | + | [[Image:1hbs.jpg|left|200px]]<br /><applet load="1hbs" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hbs" size=" | + | |
caption="1hbs, resolution 3.0Å" /> | caption="1hbs, resolution 3.0Å" /> | ||
'''REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION'''<br /> | '''REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION'''<br /> | ||
| Line 11: | Line 10: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1HBS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with HEM as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1HBS is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=HEM:'>HEM</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HBS OCA]. |
==Reference== | ==Reference== | ||
| Line 22: | Line 21: | ||
[[Category: oxygen transport]] | [[Category: oxygen transport]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:55:45 2008'' |
Revision as of 13:55, 15 February 2008
|
REFINED CRYSTAL STRUCTURE OF DEOXYHEMOGLOBIN S. I. RESTRAINED LEAST-SQUARES REFINEMENT AT 3.0-ANGSTROMS RESOLUTION
Contents |
Overview
The crystal structure of deoxyhemoglobin S has been refined at 3.0-A, resolution using the Hendrickson-Konnert restrained least-squares method., Comparison with the structure of deoxyhemoglobin A reveals a hingelike, movement of the beta-chain A helices, which are involved in molecular, contacts, toward the EF corners of their respective subunits. This, movement brings the amino termini of the beta-chains closer to the, molecular dyad. The A helices remain alpha-helical throughout their entire, lengths. No other major structural difference is found between, deoxyhemoglobin A and deoxyhemoglobin S.
Disease
Known diseases associated with this structure: Erythremias, alpha- OMIM:[141800], Erythremias, beta- OMIM:[141900], Erythrocytosis OMIM:[141850], HPFH, deletion type OMIM:[141900], Heinz body anemia OMIM:[141850], Heinz body anemias, alpha- OMIM:[141800], Heinz body anemias, beta- OMIM:[141900], Hemoglobin H disease OMIM:[141850], Hypochromic microcytic anemia OMIM:[141850], Methemoglobinemias, alpha- OMIM:[141800], Methemoglobinemias, beta- OMIM:[141900], Sickle cell anemia OMIM:[141900], Thalassemia, alpha- OMIM:[141850], Thalassemia-beta, dominant inclusion-body OMIM:[141900], Thalassemias, alpha- OMIM:[141800], Thalassemias, beta- OMIM:[141900]
About this Structure
1HBS is a Protein complex structure of sequences from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Refined crystal structure of deoxyhemoglobin S. I. Restrained least-squares refinement at 3.0-A resolution., Padlan EA, Love WE, J Biol Chem. 1985 Jul 15;260(14):8272-9. PMID:4008491
Page seeded by OCA on Fri Feb 15 15:55:45 2008
