1stp

From Proteopedia

(Difference between revisions)

Revision as of 19:04, 12 July 2016

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

Structural highlights

1stp is a 1 chain structure with sequence from As 4.1583. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SAV_STRAV] The biological function of streptavidin is not known. Forms a strong non-covalent specific complex with biotin (one molecule of biotin per subunit of streptavidin).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1stp"

Categories: As 4 1583 | Salemme, F R | Weber, P C | Biotin binding protein

@@ Line 5: / Line 5: @@
 <table><tr><td colspan='2'>[[1stp]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/As_4.1583 As 4.1583]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1STP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1STP FirstGlance]. <br>
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BTN:BIOTIN'>BTN</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1stp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1stp OCA], [http://pdbe.org/1stp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1stp RCSB], [http://www.ebi.ac.uk/pdbsum/1stp PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1stp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1stp OCA], [http://pdbe.org/1stp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1stp RCSB], [http://www.ebi.ac.uk/pdbsum/1stp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1stp ProSAT]</span></td></tr>
 </table>
 == Function ==

1stp

From Proteopedia

Revision as of 19:04, 12 July 2016

STRUCTURAL ORIGINS OF HIGH-AFFINITY BIOTIN BINDING TO STREPTAVIDIN

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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