1axi

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[[Image:1axi.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1axi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1axi OCA], [http://www.ebi.ac.uk/pdbsum/1axi PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1axi RCSB]</span>
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'''STRUCTURAL PLASTICITY AT THE HGH:HGHBP INTERFACE'''
'''STRUCTURAL PLASTICITY AT THE HGH:HGHBP INTERFACE'''
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[[Category: Vos, A M.De.]]
[[Category: Vos, A M.De.]]
[[Category: Wells, J A.]]
[[Category: Wells, J A.]]
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[[Category: complex (hormone/receptor)]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 10:48:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:49:25 2008''
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Revision as of 07:48, 2 May 2008

Image:1axi.gif

Template:STRUCTURE 1axi

STRUCTURAL PLASTICITY AT THE HGH:HGHBP INTERFACE


Overview

Remodeling of the interface between human growth hormone (hGH) and the extracellular domain of its receptor was studied by deleting a critical tryptophan residue (at position 104) in the receptor, creating a large cavity, and selecting a pentamutant of hGH by phage display that fills the cavity and largely restores binding affinity. A 2.1 A resolution x-ray structure of the mutant complex showed that the receptor cavity was filled by selected hydrophobic mutations of hGH. Large structural rearrangements occurred in the interface at sites that were distant from the mutations. Such plasticity may be a means for protein-protein interfaces to adapt to mutations as they coevolve.

About this Structure

1AXI is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural plasticity in a remodeled protein-protein interface., Atwell S, Ultsch M, De Vos AM, Wells JA, Science. 1997 Nov 7;278(5340):1125-8. PMID:9353194 Page seeded by OCA on Fri May 2 10:48:47 2008

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