1stp

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[[Image:1stp.gif|left|200px]]
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{{STRUCTURE_1stp| PDB=1stp | SCENE= }}
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'''STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN'''
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===STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN===
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==Overview==
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The high affinity of the noncovalent interaction between biotin and streptavidin forms the basis for many diagnostic assays that require the formation of an irreversible and specific linkage between biological macromolecules. Comparison of the refined crystal structures of apo and a streptavidin:biotin complex shows that the high affinity results from several factors. These factors include the formation of multiple hydrogen bonds and van der Waals interactions between biotin and the protein, together with the ordering of surface polypeptide loops that bury the biotin in the protein interior. Structural alterations at the biotin binding site produce quaternary changes in the streptavidin tetramer. These changes apparently propagate through cooperative deformations in the twisted beta sheets that link tetramer subunits.
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(as it appears on PubMed at http://www.pubmed.gov), where 2911722 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2911722}}
==About this Structure==
==About this Structure==
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[[Category: Weber, P C.]]
[[Category: Weber, P C.]]
[[Category: Biotin binding protein]]
[[Category: Biotin binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Apr 7 22:44:16 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:31:24 2008''

Revision as of 15:31, 27 July 2008


PDB ID 1stp

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1stp, resolution 2.60Å ()
Ligands:
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

Template:ABSTRACT PUBMED 2911722

About this Structure

1STP is a Single protein structure of sequence from Streptomyces avidinii. Full crystallographic information is available from OCA.

Reference

Structural origins of high-affinity biotin binding to streptavidin., Weber PC, Ohlendorf DH, Wendoloski JJ, Salemme FR, Science. 1989 Jan 6;243(4887):85-8. PMID:2911722

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